Author: "Smertenko A" / Topic: biology - Searchworks@Jio Institute Digital Library Search Results

81 results on '"Smertenko A"'

1. Brachypodium distachyon MAP20 functions in metaxylem pit development and contributes to drought recovery

Author: Glenn W. Turner, Karen A. Sanguinet, Janice de Almeida Engler, Tetyana Smertenko, Andrei Smertenko, Rhoda A. T. Brew-Appiah, Raymundo Alfaro-Aco, and Deirdre Fahy
Subjects: 0106 biological sciences, 0301 basic medicine, Physiology, Plant Science, Microtubules, 01 natural sciences, Cell wall, 03 medical and health sciences, Cell Wall, Live cell imaging, Microtubule, Drought recovery, Plant Proteins, Microtubule nucleation, biology, Chemistry, Vascular bundle, biology.organism_classification, Droughts, Cell biology, 030104 developmental biology, Microtubule Proteins, Brachypodium distachyon, Secondary cell wall, Brachypodium, 010606 plant biology & botany
Abstract: Pits are regions in the cell walls of plant tracheary elements that lack secondary walls. Each pit consists of a space within the secondary wall called a pit chamber, and a modified primary wall called the pit membrane. The pit membrane facilitates transport of solutions between vessel cells and restricts embolisms during drought. Here we analyzed the role of an angiosperm-specific TPX2-like microtubule protein MAP20 in pit formation using Brachypodium distachyon as a model system. Live cell imaging was used to analyze the interaction of MAP20 with microtubules and the impact of MAP20 on microtubule dynamics. MAP20-specific antibody was used to study expression and localization of MAP20 in different cell types during vascular bundle development. We used an artificial microRNAs (amiRNA) knockdown approach to determine the function of MAP20. MAP20 is expressed during the late stages of vascular bundle development and localizes around forming pits and under secondary cell wall thickenings in metaxylem cells. MAP20 suppresses microtubule depolymerization; however, unlike the animal TPX2 counterpart, MAP20 does not cooperate with the γ-tubulin ring complex in microtubule nucleation. Knockdown of MAP20 causes bigger pits, thinner pit membranes, perturbed vasculature development, lower reproductive potential and higher drought susceptibility. We conclude that MAP20 may contribute to drought adaptation by modulating pit size and pit membrane thickness in metaxylem.
Published: 2020

2. SELECTION EVALUATION OF INTROGRESSIVE LINES OF SOFT WINTER WHEAT WITH SIGNS OF RESISTANCE TO PHYTOPATHOGENS

Author: O.O. Molodchenkova, І.І . Motsniy, A. I. Kryvenko, L.T. Mishchenko, A.P. Smertenko, and R.V. Solomonov
Subjects: Resistance (ecology), Agronomy, Winter wheat, Plant Science, Biology, Selection (genetic algorithm)
Published: 2021

3. A guide to plant TPX2-like and WAVE-DAMPENED2-like proteins

Author: Alyssa Parish, Karl Effertz, Shaun J. Clare, Andrei Smertenko, Sharol Schmidt, and Austin Ross
Subjects: 0106 biological sciences, Cell division, Physiology, Protein domain, Arabidopsis, Cell Cycle Proteins, Plant Science, medicine.disease_cause, Microtubules, 01 natural sciences, Genome, 03 medical and health sciences, Microtubule, medicine, Review Papers, Plant Proteins, 030304 developmental biology, 0303 health sciences, Mutation, biology, Abiotic stress, biology.organism_classification, Cell biology, Peroxidases, Microtubule-Associated Proteins, Function (biology), 010606 plant biology & botany
Abstract: TPX2 proteins were first identified in vertebrates as a key mitotic spindle assembly factor. Subsequent studies demonstrated that TPX2 is an intricate protein, with functionally and structurally distinct domains and motifs including Aurora kinase-binding, importin-binding, central microtubule-binding, and C-terminal TPX2 conserved domain, among others. The first plant TPX2-like protein, WAVE-DAMPENED2, was identified in Arabidopsis as a dominant mutation responsible for reducing the waviness of roots grown on slanted agar plates. Each plant genome encodes at least one ‘canonical’ protein with all TPX2 domains and a family of proteins (20 in Arabidopsis) that diversified to contain only some of the domains. Although all plant TPX2-family proteins to date bind microtubules, they function in distinct processes such as cell division, regulation of hypocotyl cell elongation by hormones and light signals, vascular development, or abiotic stress tolerance. Consequently, their expression patterns, regulation, and functions have diverged considerably. Here we summarize the current body of knowledge surrounding plant TPX2-family proteins.
Published: 2020

4. Guidelines for the use and interpretation of assays for monitoring autophagy (4th edition) 1

Author: Klionsky, Daniel, Abdel-Aziz, Amal Kamal, Abdelfatah, Sara, Abdellatif, Mahmoud, Abdoli, Asghar, Abel, Steffen, Abeliovich, Hagai, Abildgaard, Marie, Abudu, Yakubu Princely, Acevedo-Arozena, Abraham, Adamopoulos, Iannis, Adeli, Khosrow, Adolph, Timon, Adornetto, Annagrazia, Aflaki, Elma, Agam, Galila, Agarwal, Anupam, Aggarwal, Bharat, Agnello, Maria, Agostinis, Patrizia, Agrewala, Javed, Agrotis, Alexander, Aguilar, Patricia, Ahmad, S Tariq, Ahmed, Zubair, Ahumada-Castro, Ulises, Aits, Sonja, Aizawa, Shu, Akkoc, Yunus, Akoumianaki, Tonia, Akpinar, Hafize Aysin, Al-Abd, Ahmed, Al-Akra, Lina, Al-Gharaibeh, Abeer, Alaoui-Jamali, Moulay, Alberti, Simon, Alcocer-Gómez, Elísabet, Alessandri, Cristiano, Ali, Muhammad, Alim Al-Bari, M Abdul, Aliwaini, Saeb, Alizadeh, Javad, Almacellas, Eugènia, Almasan, Alexandru, Alonso, Alicia, Alonso, Guillermo, Altan-Bonnet, Nihal, Altieri, Dario, Álvarez, Élida, Alves, Sara, Alves Da Costa, Cristine, Alzaharna, Mazen, Amadio, Marialaura, Amantini, Consuelo, Amaral, Cristina, Ambrosio, Susanna, Amer, Amal, Ammanathan, Veena, An, Zhenyi, Andersen, Stig, Andrabi, Shaida, Andrade-Silva, Magaiver, Andres, Allen, Angelini, Sabrina, Ann, David, Anozie, Uche, Ansari, Mohammad, Antas, Pedro, Antebi, Adam, Antón, Zuriñe, Anwar, Tahira, Apetoh, Lionel, Apostolova, Nadezda, Araki, Toshiyuki, Araki, Yasuhiro, Arasaki, Kohei, Araújo, Wagner, Araya, Jun, Arden, Catherine, Arévalo, Maria-Angeles, Arguelles, Sandro, Arias, Esperanza, Arikkath, Jyothi, Arimoto, Hirokazu, Ariosa, Aileen, Armstrong-James, Darius, Arnauné-Pelloquin, Laetitia, Aroca, Angeles, Arroyo, Daniela, Arsov, Ivica, Artero, Rubén, Asaro, Dalia Maria Lucia, Aschner, Michael, Ashrafizadeh, Milad, Ashur-Fabian, Osnat, Atanasov, Atanas, Au, Alicia, Auberger, Patrick, Auner, Holger, Aurelian, Laure, Autelli, Riccardo, Avagliano, Laura, Ávalos, Yenniffer, Aveic, Sanja, Aveleira, Célia Alexandra, Avin-Wittenberg, Tamar, Aydin, Yucel, Ayton, Scott, Ayyadevara, Srinivas, Azzopardi, Maria, Baba, Misuzu, Backer, Jonathan, Backues, Steven, Bae, Dong-Hun, Bae, Ok-Nam, Bae, Soo Han, Baehrecke, Eric, Baek, Ahruem, Baek, Seung-Hoon, Baek, Sung Hee, Bagetta, Giacinto, Bagniewska-Zadworna, Agnieszka, Bai, Hua, Bai, Jie, Bai, Xiyuan, Bai, Yidong, Bairagi, Nandadulal, Baksi, Shounak, Balbi, Teresa, Baldari, Cosima, Balduini, Walter, Ballabio, Andrea, Ballester, Maria, Balazadeh, Salma, Balzan, Rena, Bandopadhyay, Rina, Banerjee, Sreeparna, Banerjee, Sulagna, Bánréti, Ágnes, Bao, Yan, Baptista, Mauricio, Baracca, Alessandra, Barbati, Cristiana, Bargiela, Ariadna, Barilà, Daniela, Barlow, Peter, Barmada, Sami, Barreiro, Esther, Barreto, George, Bartek, Jiri, Bartel, Bonnie, Bartolome, Alberto, Barve, Gaurav, Basagoudanavar, Suresh, Bassham, Diane, Bast, Robert, Basu, Alakananda, Batoko, Henri, Batten, Isabella, Baulieu, Etienne, Baumgarner, Bradley, Bayry, Jagadeesh, Beale, Rupert, Beau, Isabelle, Beaumatin, Florian, Bechara, Luiz, Beck, George, Beers, Michael, Begun, Jakob, Behrends, Christian, Behrens, Georg, Bei, Roberto, Bejarano, Eloy, Bel, Shai, Behl, Christian, Belaid, Amine, Belgareh-Touzé, Naïma, Bellarosa, Cristina, Belleudi, Francesca, Belló Pérez, Melissa, Bello-Morales, Raquel, Beltran, Jackeline Soares de Oliveira, Beltran, Sebastián, Benbrook, Doris Mangiaracina, Bendorius, Mykolas, Benitez, Bruno, Benito-Cuesta, Irene, Bensalem, Julien, Berchtold, Martin, Berezowska, Sabina, Bergamaschi, Daniele, Bergami, Matteo, Bergmann, Andreas, Berliocchi, Laura, Berlioz-Torrent, Clarisse, Bernard, Amélie, Berthoux, Lionel, Besirli, Cagri, Besteiro, Sebastien, Betin, Virginie, Beyaert, Rudi, Bezbradica, Jelena, Bhaskar, Kiran, Bhatia-Kissova, Ingrid, Bhattacharya, Resham, Bhattacharya, Sujoy, Bhattacharyya, Shalmoli, Bhuiyan, Md Shenuarin, Bhutia, Sujit Kumar, Bi, Lanrong, Bi, Xiaolin, Biden, Trevor, Bijian, Krikor, Billes, Viktor, Binart, Nadine, Bincoletto, Claudia, Birgisdottir, Asa, Bjorkoy, Geir, Blanco, Gonzalo, Blas-Garcia, Ana, Blasiak, Janusz, Blomgran, Robert, Blomgren, Klas, Blum, Janice, Boada-Romero, Emilio, Boban, Mirta, Boesze-Battaglia, Kathleen, Boeuf, Philippe, Boland, Barry, Bomont, Pascale, Bonaldo, Paolo, Bonam, Srinivasa Reddy, Bonfili, Laura, Bonifacino, Juan, Boone, Brian, Bootman, Martin, Bordi, Matteo, Borner, Christoph, Bornhauser, Beat, Borthakur, Gautam, Bosch, Jürgen, Bose, Santanu, botana, luis, Botas, Juan, Boulanger, Chantal, Boulton, Michael, Bourdenx, Mathieu, Bourgeois, Benjamin, Bourke, Nollaig, Bousquet, Guilhem, Boya, Patricia, Bozhkov, Peter, Bozi, Luiz, Bozkurt, Tolga, Brackney, Doug, Brandts, Christian, Braun, Ralf, Braus, Gerhard, Bravo-Sagua, Roberto, Bravo-San Pedro, José, Brest, Patrick, Bringer, Marie-Agnès, Briones-Herrera, Alfredo, Broaddus, V Courtney, Brodersen, Peter, Brodsky, Jeffrey, Brody, Steven, Bronson, Paola, Bronstein, Jeff, Brown, Carolyn, Brown, Rhoderick, Brum, Patricia, Brumell, John, Brunetti-Pierri, Nicola, Bruno, Daniele, Bryson-Richardson, Robert, Bucci, Cecilia, Buchrieser, Carmen, Bueno, Marta, Buitrago-Molina, Laura Elisa, Buraschi, Simone, Buch, Shilpa, Buchan, J Ross, Buckingham, Erin, Budak, Hikmet, Budini, Mauricio, Bultynck, Geert, Burada, Florin, Burgoyne, Joseph, Burón, M Isabel, Bustos, Victor, Büttner, Sabrina, Butturini, Elena, Byrd, Aaron, Cabas, Isabel, Cabrera-Benitez, Sandra, Cadwell, Ken, Cai, Jingjing, Cai, Lu, Cai, Qian, Cairó, Montserrat, Calbet, Jose, Caldwell, Guy, Caldwell, Kim, Call, Jarrod, Calvani, Riccardo, Calvo, Ana, Calvo-Rubio Barrera, Miguel, Camara, Niels OS, Camonis, Jacques, Camougrand, Nadine, Campanella, Michelangelo, Campbell, Edward, Campbell-Valois, François-Xavier, Campello, Silvia, Campesi, Ilaria, Campos, Juliane, Camuzard, Olivier, Cancino, Jorge, Candido de Almeida, Danilo, Canesi, Laura, Caniggia, Isabella, Canonico, Barbara, Cantí, Carles, Cao, Bin, Caraglia, Michele, Caramés, Beatriz, Carchman, Evie, Cardenal-Muñoz, Elena, Cardenas, Cesar, Cardenas, Luis, Cardoso, Sandra, Carew, Jennifer, Carle, Georges, Carleton, Gillian, Carloni, Silvia, Carmona-Gutierrez, Didac, Carneiro, Leticia, Carnevali, Oliana, Carosi, Julian, Carra, Serena, Carrier, Alice, Carrier, Lucie, Carroll, Bernadette, Carter, A Brent, Carvalho, Andreia Neves, Casanova, Magali, Casas, Caty, Casas, Josefina, Cassioli, Chiara, Castillo, Eliseo, Castillo, Karen, Castillo-Lluva, Sonia, Castoldi, Francesca, Castori, Marco, Castro, Ariel, Castro-Caldas, Margarida, Castro-Hernandez, Javier, Castro-Obregon, Susana, Catz, Sergio, Cavadas, Claudia, Cavaliere, Federica, Cavallini, Gabriella, Cavinato, Maria, Cayuela, Maria, Cebollada Rica, Paula, Cecarini, Valentina, Cecconi, Francesco, Cechowska-Pasko, Marzanna, Cenci, Simone, Ceperuelo-Mallafré, Victòria, Cerqueira, João, Cerutti, Janete, Cervia, Davide, Cetintas, Vildan Bozok, Cetrullo, Silvia, Chae, Han-Jung, Chagin, Andrei, Chai, Chee-Yin, Chakrabarti, Gopal, Chakrabarti, Oishee, Chakraborty, Tapas, Chakraborty, Trinad, Chami, mounia, Chamilos, Georgios, Chan, David, Chan, Edmond, Chan, Edward, Chan, H.Y. Edwin, Chan, Helen, Chan, Hung, Chan, Matthew, Chan, Yau Sang, Chandra, Partha, Chang, Chih-Peng, Chang, Chunmei, Chang, Hao-Chun, Chang, Kai, Chao, Jie, Chapman, Tracey, Charlet-Berguerand, Nicolas, Chatterjee, Samrat, Chaube, Shail, Chaudhary, Anu, Chauhan, Santosh, Chaum, Edward, Checler, Frédéric, Cheetham, Michael, Chen, Chang-Shi, Chen, Guang-Chao, Chen, Jian-Fu, Chen, Liam, Chen, Leilei, Chen, Lin, Chen, Mingliang, Chen, Mu-Kuan, Chen, Ning, Chen, Quan, Chen, Ruey-Hwa, Chen, Shi, Chen, Wei, Chen, Weiqiang, Chen, Xin-Ming, Chen, Xiong-Wen, Chen, Xu, Chen, Yan, Chen, Ye-Guang, Chen, Yingyu, Chen, Yongqiang, Chen, Yu-Jen, Chen, Yue-Qin, Chen, Zhefan Stephen, Chen, Zhi, Chen, Zhi-Hua, Chen, Zhijian, Chen, Zhixiang, Cheng, Hanhua, Cheng, Jun, Cheng, Shi-Yuan, Cheng, Wei, Cheng, Xiaodong, Cheng, Xiu-Tang, Cheng, Yiyun, Cheng, Zhiyong, Chen, Zhong, Cheong, Heesun, Cheong, Jit Kong, Chernyak, Boris, Cherry, Sara, Cheung, Chi Fai Randy, Cheung, Chun Hei Antonio, Cheung, King-Ho, Chevet, Eric, Chi, Richard, Chiang, Alan Kwok Shing, Chiaradonna, Ferdinando, Chiarelli, Roberto, Chiariello, Mario, Chica, Nathalia, Chiocca, Susanna, Chiong, Mario, Chiou, Shih-Hwa, Chiramel, Abhilash, Chiurchiù, Valerio, Cho, Dong-Hyung, Choe, Seong-Kyu, Choi, Augustine, Choi, Mary, Choudhury, Kamalika Roy, Chow, Norman, Chu, Charleen, Chua, Jason, Chua, John Jia En, Chung, Hyewon, Chung, Kin Pan, Chung, Seockhoon, Chung, So-Hyang, Chung, Yuen-Li, Cianfanelli, Valentina, Ciechomska, Iwona, Cifuentes, Mariana, Cinque, Laura, Cirak, Sebahattin, Cirone, Mara, Clague, Michael, Clarke, Robert, Clementi, Emilio, Coccia, Eliana, Codogno, Patrice, Cohen, Ehud, Cohen, Mickael, Colasanti, Tania, Colasuonno, Fiorella, Colbert, Robert, Colell, Anna, Čolić, Miodrag, Coll, Nuria, Collins, Mark, Colombo, María, Colón-Ramos, Daniel, Combaret, Lydie, Comincini, Sergio, Cominetti, Márcia, Consiglio, Antonella, Conte, Andrea, Conti, Fabrizio, Contu, Viorica Raluca, Cookson, Mark, Coombs, Kevin, Coppens, Isabelle, Corasaniti, Maria Tiziana, Corkery, Dale, Cordes, Nils, Cortese, Katia, Costa, Maria do Carmo, Costantino, Sarah, Costelli, Paola, Coto-Montes, Ana, Crack, Peter, Crespo, Jose, Criollo, Alfredo, Crippa, Valeria, Cristofani, Riccardo, Csizmadia, Tamas, Cuadrado, Antonio, Cui, Bing, Cui, Jun, Cui, Yixian, Cui, Yong, Culetto, Emmanuel, Cumino, Andrea, Cybulsky, Andrey, Czaja, Mark, Czuczwar, Stanislaw, D'Adamo, Stefania, D'Amelio, Marcello, D'Arcangelo, Daniela, D'Lugos, Andrew, D'Orazi, Gabriella, da Silva, James, Dafsari, Hormos Salimi, Dagda, Ruben, Dagdas, Yasin, Daglia, Maria, Dai, Xiaoxia, Dai, Yun, Dai, Yuyuan, Dal Col, Jessica, Dalhaimer, Paul, Dalla Valle, Luisa, Dallenga, Tobias, Dalmasso, Guillaume, Damme, Markus, Dando, Ilaria, Dantuma, Nico, Darling, April, Das, Hiranmoy, Dasarathy, Srinivasan, Dasari, Santosh, Dash, Srikanta, Daumke, Oliver, Dauphinee, Adrian, Davies, Jeffrey, Dávila, Valeria, Davis, Roger, Davis, Tanja, Dayalan Naidu, Sharadha, De Amicis, Francesca, De Bosscher, Karolien, De Felice, Francesca, De Franceschi, Lucia, De Leonibus, Chiara, de Mattos Barbosa, Mayara, De Meyer, Guido, De Milito, Angelo, De Nunzio, Cosimo, De Palma, Clara, De Santi, Mauro, De Virgilio, Claudio, De Zio, Daniela, Debnath, Jayanta, DeBosch, Brian, Decuypere, Jean-Paul, Deehan, Mark, Deflorian, Gianluca, DeGregori, James, Dehay, Benjamin, Del Rio, Gabriel, Delaney, Joe, Delbridge, Lea, Delorme-Axford, Elizabeth, Delpino, M Victoria, Demarchi, Francesca, Dembitz, Vilma, Demers, Nicholas, Deng, Hongbin, Deng, Zhiqiang, Dengjel, Joern, Dent, Paul, Denton, Donna, DePamphilis, Melvin, Der, Channing, Deretic, Vojo, Descoteaux, Albert, Devis, Laura, Devkota, Sushil, Devuyst, Olivier, Dewson, Grant, Dharmasivam, Mahendiran, Dhiman, Rohan, di Bernardo, Diego, Di Cristina, Manlio, Di Domenico, Fabio, Di Fazio, Pietro, Di Fonzo, Alessio, Di Guardo, Giovanni, Di Guglielmo, Gianni, Di Leo, Luca, Di Malta, Chiara, Di Nardo, Alessia, Di Rienzo, Martina, Di Sano, Federica, Diallinas, George, Diao, Jiajie, Diaz-Araya, Guillermo, Díaz-Laviada, Inés, Dickinson, Jared, Diederich, Marc, Dieudé, Mélanie, Dikic, Ivan, Ding, Shiping, Ding, Wen-Xing, Dini, Luciana, Dinić, Jelena, Dinic, Miroslav, Dinkova-Kostova, Albena, Dionne, Marc, Distler, Jörg, Diwan, Abhinav, Dixon, Ian, Djavaheri-Mergny, Mojgan, Dobrinski, Ina, Dobrovinskaya, Oxana, Dobrowolski, Radek, Dobson, Renwick, Đokić, Jelena, Dokmeci Emre, Serap, Donadelli, Massimo, Dong, Bo, Dong, Xiaonan, Dong, Zhiwu, Dorn Ii, Gerald, Dotsch, Volker, Dou, Huan, Dou, Juan, Dowaidar, Moataz, Dridi, Sami, Drucker, Liat, Du, Ailian, Du, Caigan, Du, Guangwei, Du, Hai-Ning, Du, Li-Lin, du Toit, André, Duan, Shao-Bin, Duan, Xiaoqiong, Duarte, Sónia, Dubrovska, Anna, Dunlop, Elaine, Dupont, Nicolas, Durán, Raúl, Dwarakanath, Bilikere, Dyshlovoy, Sergey, Ebrahimi-Fakhari, Darius, Eckhart, Leopold, Edelstein, Charles, Efferth, Thomas, Eftekharpour, Eftekhar, Eichinger, Ludwig, Eid, Nabil, Eisenberg, Tobias, Eissa, N Tony, Eissa, Sanaa, Ejarque, Miriam, El Andaloussi, Abdeljabar, El-Hage, Nazira, El-Naggar, Shahenda, Eleuteri, Anna Maria, El-Shafey, Eman, Elgendy, Mohamed, Eliopoulos, Aristides, Elizalde, María, Elks, Philip, Elsasser, Hans-Peter, Elsherbiny, Eslam, Emerling, Brooke, Emre, N., Eng, Christina, Engedal, Nikolai, Engelbrecht, Anna-Mart, Engelsen, Agnete, Enserink, Jorrit, Escalante, Ricardo, Esclatine, Audrey, Escobar-Henriques, Mafalda, Eskelinen, Eeva-Liisa, Espert, Lucile, Eusebio, Makandjou-Ola, Fabrias, Gemma, Fabrizi, Cinzia, Facchiano, Antonio, Facchiano, Francesco, Fadeel, Bengt, Fader, Claudio, Faesen, Alex, Fairlie, W Douglas, Falcó, Alberto, Falkenburger, Bjorn, Fan, Daping, Fan, Jie, Fan, Yanbo, Fang, Evandro, Fang, Yanshan, Fang, Yognqi, Fanto, Manolis, Farfel-Becker, Tamar, Faure, Mathias, Fazeli, Gholamreza, Fedele, Anthony, Feldman, Arthur, Feng, Du, Feng, Jiachun, Feng, Lifeng, Feng, Yibin, Feng, Yuchen, Feng, Wei, Fenz Araujo, Thais, Ferguson, Thomas, Fernández, Álvaro, Fernandez-Checa, Jose, Fernández-Veledo, Sonia, Fernie, Alisdair, Ferrante, Anthony, Ferraresi, Alessandra, Ferrari, Merari, Ferreira, Julio, Ferro-Novick, Susan, Figueras, Antonio, Filadi, Riccardo, Filigheddu, Nicoletta, Filippi-Chiela, Eduardo, Filomeni, Giuseppe, Fimia, Gian Maria, Fineschi, Vittorio, Finetti, Francesca, Finkbeiner, Steven, Fisher, Edward, Fisher, Paul, Flamigni, Flavio, Fliesler, Steven, Flo, Trude, Florance, Ida, Florey, Oliver, Florio, Tullio, Fodor, Erika, Follo, Carlo, Fon, Edward, Forlino, Antonella, Fornai, Francesco, Fortini, Paola, Fracassi, Anna, Fraldi, Alessandro, Franco, Brunella, Franco, Rodrigo, Franconi, Flavia, Frankel, Lisa, Friedman, Scott, Fröhlich, Leopold, Frühbeck, Gema, Fuentes, Jose, Fujiki, Yukio, Fujita, Naonobu, Fujiwara, Yuuki, Fukuda, Mitsunori, Fulda, Simone, Furic, Luc, Furuya, Norihiko, Fusco, Carmela, Gack, Michaela, Gaffke, Lidia, Galadari, Sehamuddin, Galasso, Alessia, Galindo, Maria, Gallolu Kankanamalage, Sachith, Galluzzi, Lorenzo, Galy, Vincent, Gammoh, Noor, Gan, Boyi, Ganley, Ian, Gao, Feng, Gao, Hui, Gao, Minghui, Gao, Ping, Gao, Shou-Jiang, Gao, Wentao, Gao, Xiaobo, Garcera, Ana, Garcia, Maria Noé, Garcia, Verónica, García-del Portillo, Francisco, Garcia-Escudero, Vega, Garcia-Garcia, Aracely, Garcia-Macia, Marina, García-Moreno, Diana, Garcia-Ruiz, Carmen, García-Sanz, Patricia, Garg, Abhishek, Gargini, Ricardo, Garofalo, Tina, Garry, Robert, Gassen, Nils, Gatica, Damian, Ge, Liang, Ge, Wanzhong, Geiss-Friedlander, Ruth, Gelfi, Cecilia, Genschik, Pascal, Gentle, Ian, Gerbino, Valeria, Gerhardt, Christoph, Germain, Kyla, Germain, Marc, Gewirtz, David, Ghasemipour Afshar, Elham, Ghavami, Saeid, Ghigo, Alessandra, Ghosh, Manosij, Giamas, Georgios, Giampietri, Claudia, Giatromanolaki, Alexandra, Gibson, Gary, Gibson, Spencer, Ginet, Vanessa, Giniger, Edward, Giorgi, Carlotta, Girao, Henrique, Girardin, Stephen, Giridharan, Mridhula, Giuliano, Sandy, Giulivi, Cecilia, Giuriato, Sylvie, Giustiniani, Julien, Gluschko, Alexander, Goder, Veit, Goginashvili, Alexander, Golab, Jakub, Goldstone, David, Golebiewska, Anna, Gomes, Luciana, Gomez, Rodrigo, Gómez-Sánchez, Rubén, Gomez-Puerto, Maria Catalina, Gomez-Sintes, Raquel, Gong, Qingqiu, Goni, Felix, González-Gallego, Javier, Gonzalez-Hernandez, Tomas, Gonzalez-Polo, Rosa, Gonzalez-Reyes, Jose, González-Rodríguez, Patricia, Goping, Ing Swie, Gorbatyuk, Marina, Gorbunov, Nikolai, Görgülü, Kıvanç, Gorojod, Roxana, Gorski, Sharon, Goruppi, Sandro, Gotor, Cecilia, Gottlieb, Roberta, Gozes, Illana, Gozuacik, Devrim, Graef, Martin, Gräler, Markus, Granatiero, Veronica, Grasso, Daniel, Gray, Joshua, Green, Douglas, Greenhough, Alexander, Gregory, Stephen, Griffin, Edward, Grinstaff, Mark, Gros, Frederic, Grose, Charles, Gross, Angelina, Gruber, Florian, Grumati, Paolo, Grune, Tilman, Gu, Xueyan, Guan, Jun-Lin, Guardia, Carlos, Guda, Kishore, Guerra, Flora, Guerri, Consuelo, Guha, Prasun, Guillén, Carlos, Gujar, Shashi, Gukovskaya, Anna, Gukovsky, Ilya, Gunst, Jan, Günther, Andreas, Guntur, Anyonya, Guo, Chuanyong, Guo, Chun, Guo, Hongqing, Guo, Lian-Wang, Guo, Ming, Gupta, Pawan, Gupta, Shashi Kumar, Gupta, Swapnil, Gupta, Veer Bala, Gupta, Vivek, Gustafsson, Asa, Gutterman, David, H B, Ranjitha, Haapasalo, Annakaisa, Haber, James, Hać, Aleksandra, Hadano, Shinji, Hafrén, Anders, Haidar, Mansour, Hall, Belinda, Halldén, Gunnel, Hamacher-Brady, Anne, Hamann, Andrea, Hamasaki, Maho, Han, Weidong, Hansen, Malene, Hanson, Phyllis, Hao, Zijian, Harada, Masaru, Harhaji-Trajkovic, Ljubica, Hariharan, Nirmala, Haroon, Nigil, Harris, James, Hasegawa, Takafumi, Hasima Nagoor, Noor, Haspel, Jeffrey, Haucke, Volker, Hawkins, Wayne, Hay, Bruce, Haynes, Cole, Hayrabedyan, Soren, Hays, Thomas, He, Congcong, He, Qin, He, Rong-Rong, He, You-Wen, He, Yu-Ying, Heakal, Yasser, Heberle, Alexander, Hejtmancik, J Fielding, Helgason, Gudmundur Vignir, Henkel, Vanessa, Herb, Marc, Hergovich, Alexander, Herman-Antosiewicz, 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Karolina, Piya, Sujan, Pizzo, Paola, Plantinga, Theo, Platta, Harald, Plaza-Zabala, Ainhoa, Plomann, Markus, Plotnikov, Egor, Plun-Favreau, Helene, Pluta, Ryszard, Pocock, Roger, Pöggeler, Stefanie, Pohl, Christian, Poirot, Marc, Poletti, Angelo, Ponpuak, Marisa, Popelka, Hana, Popova, Blagovesta, Porta, Helena, Porte Alcon, Soledad, Portilla-Fernandez, Eliana, Post, Martin, Potts, Malia, Poulton, Joanna, Powers, Ted, Prahlad, Veena, Prajsnar, Tomasz, Praticò, Domenico, Prencipe, Rosaria, Priault, Muriel, Proikas-Cezanne, Tassula, Promponas, Vasilis, Proud, Christopher, Puertollano, Rosa, Puglielli, Luigi, Pulinilkunnil, Thomas, Puri, Deepika, Puri, Rajat, Puyal, Julien, Qi, Xiaopeng, Qi, Yongmei, Qian, Wenbin, Qiang, Lei, Qiu, Yu, Quadrilatero, Joe, Quarleri, Jorge, Raben, Nina, Rabinowich, Hannah, Ragona, Debora, Ragusa, Michael, Rahimi, Nader, Rahmati, Marveh, Raia, Valeria, Raimundo, Nuno, Rajasekaran, Namakkal-Soorappan, Ramachandra Rao, Sriganesh, Rami, Abdelhaq, Ramírez-Pardo, Ignacio, Ramsden, David, Randow, Felix, Rangarajan, Pundi, Ranieri, Danilo, Rao, Hai, Rao, Lang, Rao, Rekha, Rathore, Sumit, Ratnayaka, J Arjuna, Ratovitski, Edward, Ravanan, Palaniyandi, Ravegnini, Gloria, Ray, Swapan, Razani, Babak, Rebecca, Vito, Reggiori, Fulvio, Régnier-Vigouroux, Anne, Reichert, Andreas, Reigada, David, Reiling, Jan, Rein, Theo, Reipert, Siegfried, Rekha, Rokeya Sultana, Ren, Hongmei, Ren, Jun, Ren, Weichao, Renault, Tristan, Renga, Giorgia, Reue, Karen, Rewitz, Kim, Ribeiro de Andrade Ramos, Bruna, Riazuddin, S Amer, Ribeiro-Rodrigues, Teresa, Ricci, Jean-Ehrland, Ricci, Romeo, Riccio, Victoria, Richardson, Des, Rikihisa, Yasuko, Risbud, Makarand, Risueño, Ruth, Ritis, Konstantinos, Rizza, Salvatore, Rizzuto, Rosario, Roberts, Helen, Roberts, Luke, Robinson, Katherine, Roccheri, Maria Carmela, Rocchi, Stephane, Rodney, George, Rodrigues, Tiago, Rodrigues Silva, Vagner Ramon, Rodriguez, Amaia, Rodriguez-Barrueco, Ruth, Rodriguez-Henche, Nieves, Rodriguez-Rocha, Humberto, Roelofs, Jeroen, Rogers, Robert, Rogov, Vladimir, ROJO, Ana, Rolka, Krzysztof, Romanello, Vanina, Romani, Luigina, Romano, Alessandra, Romano, Patricia, Romeo-Guitart, David, Romero, Luis, Romero, Montserrat, Roney, Joseph, Rongo, Christopher, Roperto, Sante, Rosenfeldt, Mathias, Rosenstiel, Philip, Rosenwald, Anne, Roth, Kevin, Roth, Lynn, Roth, Steven, Rouschop, Kasper, Roussel, Benoit, Roux, Sophie, Rovere-Querini, Patrizia, Roy, Ajit, Rozieres, Aurore, Ruano, Diego, Rubinsztein, David, Rubtsova, Maria, Ruckdeschel, Klaus, Ruckenstuhl, Christoph, Rudolf, Emil, Rudolf, Rüdiger, Ruggieri, Alessandra, Ruparelia, Avnika Ashok, Rusmini, Paola, Russell, Ryan, Russo, Gian Luigi, Russo, Maria, Russo, Rossella, Ryabaya, Oxana, Ryan, Kevin, Ryu, Kwon-Yul, Sabater-Arcis, Maria, Sachdev, Ulka, Sacher, Michael, Sachse, Carsten, Sadhu, Abhishek, Sadoshima, Junichi, Safren, Nathaniel, Saftig, Paul, Sagona, Antonia, Sahay, Gaurav, Sahebkar, Amirhossein, Sahin, Mustafa, Sahin, Ozgur, Sahni, Sumit, Saito, Nayuta, Saito, Shigeru, Saito, Tsunenori, Sakai, Ryohei, Sakai, Yasuyoshi, Sakamaki, Jun-Ichi, Saksela, Kalle, Salazar, Gloria, Salazar-Degracia, Anna, Salekdeh, Ghasem, Saluja, Ashok, Sampaio-Marques, Belém, Sanchez, Maria Cecilia, Sanchez-Alcazar, Jose, Sanchez-Vera, Victoria, Sancho-Shimizu, Vanessa, Sanderson, J Thomas, Sandri, Marco, Santaguida, Stefano, Santambrogio, Laura, Santana, Magda, Santoni, Giorgio, Sanz, Alberto, Sanz, Pascual, Saran, Shweta, Sardiello, Marco, Sargeant, Timothy, Sarin, Apurva, Sarkar, Chinmoy, Sarkar, Sovan, Sarrias, Maria-Rosa, Sarkar, Surajit, Sarmah, Dipanka Tanu, Sarparanta, Jaakko, Sathyanarayan, Aishwarya, Sathyanarayanan, Ranganayaki, Scaglione, K Matthew, Scatozza, Francesca, Schaefer, Liliana, Schafer, Zachary, Schaible, Ulrich, Schapira, Anthony, Scharl, Michael, Schatzl, Hermann, Schein, Catherine, Scheper, Wiep, Scheuring, David, Schiaffino, Maria Vittoria, Schiappacassi, Monica, Schindl, Rainer, Schlattner, Uwe, Schmidt, Oliver, Schmitt, Roland, Schmidt, Stephen, Schmitz, Ingo, Schmukler, Eran, Schneider, Anja, Schneider, Bianca, Schober, Romana, Schoijet, Alejandra, Schott, Micah, Schramm, Michael, Schröder, Bernd, Schuh, Kai, Schüller, Christoph, Schulze, Ryan, Schürmanns, Lea, Schwamborn, Jens, Schwarten, Melanie, Scialo, Filippo, Sciarretta, Sebastiano, Scott, Melanie, Scotto, Kathleen, Scovassi, A Ivana, Scrima, Andrea, Scrivo, Aurora, Sebastian, David, Sebti, Salwa, Sedej, Simon, Segatori, Laura, Segev, Nava, Seglen, Per, Seiliez, Iban, Seki, Ekihiro, Selleck, Scott, Sellke, Frank, Selsby, Joshua, Sendtner, Michael, Senturk, Serif, Seranova, Elena, Sergi, Consolato, Serra-Moreno, Ruth, Sesaki, Hiromi, Settembre, Carmine, Setty, Subba Rao Gangi, Sgarbi, Gianluca, Sha, Ou, Shacka, John, Shah, Javeed, Shang, Dantong, Shao, Changshun, Shao, Feng, Sharbati, Soroush, Sharkey, Lisa, Sharma, Dipali, Sharma, Gaurav, Sharma, Kulbhushan, Sharma, Pawan, Sharma, Surendra, Shen, Han-Ming, Shen, Hongtao, Shen, Jiangang, Shen, Ming, Shen, Weili, Shen, Zheni, Sheng, Rui, Sheng, Zhi, Sheng, Zu-Hang, Shi, Jianjian, Shi, Xiaobing, Shi, Ying-Hong, Shiba-Fukushima, Kahori, Shieh, Jeng-Jer, Shimada, Yohta, Shimizu, Shigeomi, Shimozawa, Makoto, Shintani, Takahiro, Shoemaker, Christopher, Shojaei, Shahla, Shoji, Ikuo, Shravage, Bhupendra, Shridhar, Viji, Shu, Chih-Wen, Shu, Hong-Bing, Shui, Ke, Shukla, Arvind, Shutt, Timothy, Sica, Valentina, Siddiqui, Aleem, Sierra, Amanda, Sierra-Torre, Virginia, Signorelli, Santiago, Sil, Payel, Silva, Bruno, Silva, Johnatas, Silva-Pavez, Eduardo, Silvente-Poirot, Sandrine, Simmonds, Rachel, Simon, Anna Katharina, Simon, Hans-Uwe, Simons, Matias, Singh, Anurag, Singh, Lalit, Singh, Rajat, Singh, Shivendra, Singh, Shrawan, Singh, Sudha, Singh, Sunaina, Singh, Surinder Pal, Sinha, Debasish, Sinha, Rohit Anthony, Sinha, Sangita, Sirko, Agnieszka, Sirohi, Kapil, Sivridis, Efthimios, Skendros, Panagiotis, Skirycz, Aleksandra, Slaninová, Iva, Smaili, Soraya, Smertenko, Andrei, Smith, Matthew, Soenen, Stefaan, Sohn, Eun Jung, Sok, Sophia, Solaini, Giancarlo, Soldati, Thierry, Soleimanpour, Scott, Soler, Rosa, Solovchenko, Alexei, Somarelli, Jason, Sonawane, Avinash, Song, Fuyong, Song, Hyun Kyu, Song, Ju-Xian, Song, Kunhua, Song, Zhiyin, Soria, Leandro, Sorice, Maurizio, Soukas, Alexander, Soukup, Sandra-Fausia, Sousa, Diana, Sousa, Nadia, Spagnuolo, Paul, Spector, Stephen, Srinivas Bharath, M., St Clair, Daret, Stagni, Venturina, Staiano, Leopoldo, Stalnecker, Clint, Stankov, Metodi, Stathopulos, Peter, Stefan, Katja, Stefan, Sven Marcel, Stefanis, Leonidas, Steffan, Joan, Steinkasserer, Alexander, Stenmark, Harald, Sterneckert, Jared, Stevens, Craig, Stoka, Veronika, Storch, Stephan, Stork, Björn, Strappazzon, Flavie, Strohecker, Anne Marie, Stupack, Dwayne, Su, Huanxing, Su, Ling-Yan, Su, Longxiang, Suarez-Fontes, Ana, Subauste, Carlos, Subbian, Selvakumar, Subirada, Paula, Sudhandiran, Ganapasam, Sue, Carolyn, Sui, Xinbing, Summers, Corey, Sun, Guangchao, Sun, Jun, SUN, Kang, Sun, Meng-xiang, Sun, Qiming, Sun, Yi, Sun, Zhongjie, Sunahara, Karen, Sundberg, Eva, Susztak, Katalin, Sutovsky, Peter, Suzuki, Hidekazu, Sweeney, Gary, Symons, J David, Sze, Stephen Cho Wing, Szewczyk, Nathaniel, Tabęcka-Łonczynska, Anna, Tabolacci, Claudio, Tacke, Frank, Taegtmeyer, Heinrich, Tafani, Marco, Tagaya, Mitsuo, Tai, Haoran, Tait, Stephen, Takahashi, Yoshinori, Takats, Szabolcs, Talwar, Priti, Tam, Chit, Tam, Shing Yau, Tampellini, Davide, Tamura, Atsushi, Tan, Chong Teik, Tan, Eng-King, Tan, Ya-Qin, Tanaka, Masaki, Tanaka, Motomasa, Tang, Daolin, Tang, Jingfeng, Tang, Tie-Shan, Tanida, Isei, Tao, Zhipeng, Taouis, Mohammed, Tatenhorst, Lars, Tavernarakis, Nektarios, Taylor, Allen, Taylor, Gregory, Taylor, Joan, Tchetina, Elena, Tee, Andrew, Tegeder, Irmgard, Teis, David, Teixeira, Natercia, Teixeira-Clerc, Fatima, Tekirdag, Kumsal, Tencomnao, Tewin, Tenreiro, Sandra, Tepikin, Alexei, Testillano, Pilar, Tettamanti, Gianluca, Tharaux, Pierre-Louis, Thedieck, Kathrin, Thekkinghat, Arvind, Thellung, Stefano, Thinwa, Josephine, Thirumalaikumar, V.P., Thomas, Sufi Mary, Thomes, Paul, Thorburn, Andrew, Thukral, Lipi, Thum, Thomas, Thumm, Michael, Tian, Ling, Tichy, Ales, Till, Andreas, Timmerman, Vincent, Titorenko, Vladimir, Todi, Sokol, Todorova, Krassimira, Toivonen, Janne, Tomaipitinca, Luana, Tomar, Dhanendra, Tomas-Zapico, Cristina, Tomić, Sergej, Tong, Benjamin Chun-Kit, Tong, Chao, Tong, Xin, Tooze, Sharon, Torgersen, Maria, Torii, Satoru, Torres-López, Liliana, Torriglia, Alicia, Towers, Christina, Towns, Roberto, Toyokuni, Shinya, Trajkovic, Vladimir, Tramontano, Donatella, Tran, Quynh-Giao, Travassos, Leonardo, Trelford, Charles, Tremel, Shirley, Trougakos, Ioannis, Tsao, Betty, Tschan, Mario, Tse, Hung-Fat, Tse, Tak Fu, Tsugawa, Hitoshi, Tsvetkov, Andrey, Tumbarello, David, Tumtas, Yasin, Tuñón, María, Turcotte, Sandra, Turk, Boris, Turk, Vito, Turner, Bradley, Tuxworth, Richard, Tyler, Jessica, Tyutereva, Elena, Uchiyama, Yasuo, Ugun-Klusek, Aslihan, Uhlig, Holm, Ułamek-Kozioł, Marzena, Ulasov, Ilya, Umekawa, Midori, Ungermann, Christian, Unno, Rei, Urbe, Sylvie, Uribe-Carretero, Elisabet, Üstün, Suayib, Uversky, Vladimir, Vaccari, Thomas, Vaccaro, Maria, Vahsen, Björn, Vakifahmetoglu-Norberg, Helin, Valdor, Rut, Valente, Maria, Valko, Ayelén, Vallee, Richard, Valverde, Angela, Van Den Berghe, Greet, van der Veen, Stijn, Van Kaer, Luc, van Loosdregt, Jorg, van Wijk, Sjoerd, Vandenberghe, Wim, Vanhorebeek, Ilse, Vannier-Santos, Marcos, Vannini, Nicola, Vanrell, M Cristina, Vantaggiato, Chiara, Varano, Gabriele, Varela-Nieto, Isabel, Varga, Máté, Vasconcelos, M Helena, Vats, Somya, Vavvas, Demetrios, Vega-Naredo, Ignacio, Vega-Rubin-de-Celis, Silvia, Velasco, Guillermo, Velázquez, Ariadna, Vellai, Tibor, Vellenga, Edo, Velotti, Francesca, Verdier, Mireille, Verginis, Panayotis, Vergne, Isabelle, Verkade, Paul, Verma, Manish, Verstreken, Patrik, Vervliet, Tim, Vervoorts, Jörg, Vessoni, Alexandre, Victor, Victor, Vidal, Michel, Vidoni, Chiara, Vieira, Otilia, Vierstra, Richard, Viganó, Sonia, Vihinen, Helena, Vijayan, Vinoy, Vila, Miquel, Vilar, Marçal, Villalba, José, Villalobo, Antonio, Villarejo-Zori, Beatriz, Villarroya, Francesc, Villarroya, Joan, Vincent, Olivier, Vindis, Cecile, Viret, Christophe, Viscomi, Maria Teresa, Visnjic, Dora, Vitale, Ilio, Vocadlo, David, Voitsekhovskaja, Olga, Volonté, Cinzia, Volta, Mattia, Vomero, Marta, Von Haefen, Clarissa, Vooijs, Marc, Voos, Wolfgang, Vucicevic, Ljubica, Wade-Martins, Richard, Waguri, Satoshi, Waite, Kenrick, Wakatsuki, Shuji, Walker, David, Walker, Mark, Walker, Simon, Walter, Jochen, Wandosell, Francisco, Wang, Bo, Wang, Chao-Yung, Wang, Chen, Wang, Chenran, Wang, Chenwei, Wang, Cun-Yu, Wang, Dong, Wang, Fangyang, Wang, Feng, Wang, Fengming, Wang, Guansong, Wang, Han, Wang, Hao, Wang, Hexiang, Wang, Hong-Gang, Wang, Jianrong, Wang, Jigang, Wang, Jiou, Wang, Jundong, Wang, Kui, Wang, Lianrong, Wang, Liming, Wang, Maggie Haitian, Wang, Meiqing, Wang, Nanbu, Wang, PengWei, Wang, PeiPei, Wang, Ping, Wang, Qing Jun, Wang, Qing, Wang, Qing Kenneth, Wang, Qiong, Wang, Wen-Tao, Wang, Wuyang, Wang, Xinnan, Wang, Xuejun, Wang, Yan, Wang, Yanchang, Wang, Yanzhuang, Wang, Yen-Yun, Wang, Yihua, Wang, Yipeng, Wang, Yu, wang, yuqi, Wang, Zhe, Wang, Zhenyu, Wang, Zhouguang, Warnes, Gary, Warnsmann, Verena, Watada, Hirotaka, Watanabe, Eizo, Watchon, Maxinne, Wawrzyńska, Anna, Weaver, Timothy, Wegrzyn, Grzegorz, Wehman, Ann, Wei, Huafeng, Wei, Lei, Wei, Taotao, Wei, Yongjie, Weiergräber, Oliver, Weihl, Conrad, Weindl, Günther, Weiskirchen, Ralf, Wells, Alan, Wen, Runxia, Wen, Xin, Werner, Antonia, Weykopf, Beatrice, Wheatley, Sally, Whitton, J Lindsay, Whitworth, Alexander, Wiktorska, Katarzyna, Wildenberg, Manon, Wileman, Tom, Wilkinson, Simon, Willbold, Dieter, Williams, Brett, Williams, Robin, Williams, Roger, Williamson, Peter, Wilson, Richard, Winner, Beate, Winsor, Nathaniel, Witkin, Steven, Wodrich, Harald, Woehlbier, Ute, Wollert, Thomas, Wong, Esther, Wong, Jack Ho, Wong, Richard, Wong, Vincent Kam Wai, Wong, W Wei-Lynn, Wu, An-Guo, Wu, Chengbiao, Wu, Jian, Wu, Junfang, Wu, Kenneth, Wu, Min, Wu, Shan-Ying, Wu, Shengzhou, Wu, Shu-Yan, Wu, Shufang, Wu, William, Wu, Xiaohong, Wu, Xiaoqing, Wu, Yao-Wen, Wu, Yihua, Xavier, Ramnik, Xia, Hongguang, Xia, Lixin, Xia, Zhengyuan, Xiang, Ge, Xiang, Jin, Xiang, Mingliang, Xiang, Wei, Xiao, Bin, Xiao, Guozhi, Xiao, Hengyi, Xiao, Hong-tao, Xiao, Jian, Xiao, Lan, Xiao, Shi, Xiao, Yin, Xie, Baoming, Xie, Chuan-Ming, Xie, Min, Xie, Yuxiang, Xie, Zhiping, Xie, Zhonglin, Xilouri, Maria, Xu, Congfeng, Xu, En, Xu, Haoxing, Xu, Jing, Xu, Jinrong, Xu, Liang, Xu, Wen Wen, Xu, Xiulong, Xue, Yu, Yakhine-Diop, Sokhna, Yamaguchi, Masamitsu, Yamaguchi, Osamu, Yamamoto, Ai, Yamashina, Shunhei, Yan, Shengmin, Yan, Shian-Jang, Yan, Zhen, Yanagi, Yasuo, Yang, Chuanbin, Yang, Dun-Sheng, Yang, Huan, Yang, Huang-Tian, Yang, Hui, Yang, Jin-Ming, Yang, Jing, Yang, Jingyu, Yang, Ling, Yang, Liu, Yang, Ming, Yang, Pei-Ming, Yang, Qian, Yang, Seungwon, Yang, Shu, Yang, Shun-Fa, Yang, Wannian, Yang, Wei Yuan, Yang, Xiaoyong, Yang, Xuesong, Yang, Yi, Yang, Ying, Yao, Honghong, Yao, Shenggen, Yao, Xiaoqiang, Yao, Yong-Gang, Yao, Yong-Ming, Yasui, Takahiro, Yazdankhah, Meysam, Yen, Paul, Yi, Cong, Yin, Xiao-Ming, Yin, Yanhai, Yin, Zhangyuan, Yin, Ziyi, Ying, Meidan, Ying, Zheng, Yip, Calvin, Yiu, Stephanie Pei Tung, Yoo, Young, Yoshida, Kiyotsugu, Yoshii, Saori, Yoshimori, Tamotsu, Yousefi, Bahman, Yu, Boxuan, Yu, Haiyang, Yu, Jun, Yu, Li, Yu, Ming-Lung, Yu, Seong-Woon, Yu, Victor, Yu, W Haung, Yu, Zhengping, Yu, Zhou, Yuan, Junying, Yuan, Ling-Qing, Yuan, Shilin, Yuan, Shyng-Shiou, Yuan, Yanggang, Yuan, Zengqiang, Yue, Jianbo, Yue, Zhenyu, Yun, Jeanho, Yung, Raymond, Zacks, David, Zaffagnini, Gabriele, Zambelli, Vanessa, Zanella, Isabella, Zang, Qun, Zanivan, Sara, Zappavigna, Silvia, Zaragoza, Pilar, Zarbalis, Konstantinos, Zarebkohan, Amir, Zarrouk, Amira, Zeitlin, Scott, Zeng, Jialiu, Zeng, Ju-deng, Žerovnik, Eva, Zhan, Lixuan, Zhang, Bin, Zhang, Donna, Zhang, Hanlin, Zhang, Hong, Zhang, Honghe, Zhang, Huafeng, Zhang, Huaye, Zhang, Hui, Zhang, Hui-Ling, Zhang, Jianbin, Zhang, Jianhua, Zhang, Jing-Pu, Zhang, Kalin, Zhang, Leshuai, Zhang, Lin, Zhang, Lisheng, Zhang, Lu, Zhang, Luoying, Zhang, Menghuan, Zhang, Peng, Zhang, Sheng, Zhang, Wei, Zhang, Xiangnan, Zhang, Xiao-Wei, Zhang, Xiaolei, Zhang, Xiaoyan, Zhang, Xin, Zhang, Xinxin, Zhang, Xu Dong, Zhang, Yang, Zhang, Yanjin, Zhang, Yi, Zhang, Ying-Dong, Zhang, Yingmei, Zhang, Yuan-Yuan, Zhang, Yuchen, Zhang, Zhe, Zhang, Zhengguang, Zhang, Zhibing, Zhang, Zhihai, Zhang, Zhiyong, Zhang, Zili, Zhao, Haobin, Zhao, Lei, Zhao, Shuang, Zhao, Tongbiao, Zhao, Xiao-Fan, Zhao, Ying, Zhao, Yongchao, Zhao, Yongliang, Zhao, Yuting, Zheng, Guoping, Zheng, Kai, Zheng, Ling, Zheng, Shizhong, Zheng, Xi-Long, Zheng, Yi, Zheng, Zu-Guo, Zhivotovsky, Boris, Zhong, Qing, Zhou, Ao, Zhou, Ben, Zhou, Cefan, ZHOU, Gang, Zhou, Hao, Zhou, Hong, Zhou, Hongbo, Zhou, Jie, Zhou, Jing, Zhou, Jiyong, Zhou, Kailiang, Zhou, Rongjia, Zhou, Xu-jie, Zhou, Yanshuang, Zhou, Yinghong, Zhou, Yubin, Zhou, Zheng-Yu, Zhou, Zhou, Zhu, Binglin, Zhu, Changlian, Zhu, Guo-Qing, Zhu, Haining, Zhu, Hongxin, Zhu, Hua, Zhu, Wei-Guo, Zhu, Yanping, Zhu, Yushan, Zhuang, Haixia, Zhuang, Xiaohong, Zientara-Rytter, Katarzyna, Zimmermann, Christine, Ziviani, Elena, Zoladek, Teresa, Zong, Wei-Xing, Zorov, Dmitry, Zorzano, Antonio, Zou, Weiping, Zou, Zhen, Zou, Zhengzhi, Zuryn, Steven, Zwerschke, Werner, Brand-Saberi, Beate, Dong, X Charlie, Kenchappa, Chandra Shekar, Li, Zuguo, Lin, Yong, Oshima, Shigeru, Rong, Yueguang, Sluimer, Judith, Stallings, Christina, Tong, Chun-Kit, Ahmad, S. Tariq, Alim Al-Bari, M. Abdul, Bechara, Luiz R.G., Behrens, Georg M.N., Bhuiyan, Md. Shenuarin, Broaddus, V. Courtney, Buchan, J. Ross, Burón, M. Isabel, Carter, A. Brent, Chan, Matthew T.V., Choi, Augustine M.K., D’Adamo, Stefania, D’Amelio, Marcello, D’Arcangelo, Daniela, D’Lugos, Andrew, D’Orazi, Gabriella, De Meyer, Guido R.Y., Delpino, M. Victoria, Distler, Jörg H.W., Dixon, Ian M.C., Dobson, Renwick C.J., 2nd Dorn, Gerald, Eissa, N. Tony, Engelsen, Agnete S.T., Fairlie, W. Douglas, Ferreira, Julio C.B., H.B., Ranjitha, Hanson, Phyllis I., Hejtmancik, J. Fielding, Ho, Idy H.T., Hobbs, G. Aaron, Hoet, Peter H.M., Huang, Michael L.H., Iyer, Anand Krishnan V., Johnson, Gail V.W., Joosten, Leo A.B., Karim, Md. Razaul, Kaufmann, Stefan H.E., Ko, Ben C.B., Leck, Lionel Y.W., Lima, Thania R.R., Livingston, J. Andrew, Martin, Alexandre P.J., Montes, L. Ruth, Murphy, J. Patrick, Ng, Charlene C.W., Nicolao, M. Celeste, O’Donovan, Tracey, O’Leary, Seónadh, O’Rourke, Eyleen, O’Sullivan, Mary, O’Sullivan, Timothy, Omary, M. Bishr, Pereira, Gustavo J.S., Ratnayaka, J. Arjuna, Riazuddin, S. Amer, Rouschop, Kasper M.A., Sanderson, J. Thomas, Scaglione, K. Matthew, Schapira, Anthony H.V., Scovassi, A. Ivana, St. Clair, Daret, Sunahara, Karen K.S., Symons, J. David, Triola, Gemma, van Wijk, Sjoerd J.L., Vanrell, M. Cristina, Vasconcelos, M. Helena, Whitton, J. Lindsay, Williams, Robin S.B., Wong, W. Wei-Lynn, Wu, William K.K., Yakhine-Diop, Sokhna M.S., Yu, W. Haung, Zhang, Kalin Y.B., Dong, X. Charlie, Ain Shams University [ASU], Johannes Gutenberg - Universität Mainz = Johannes Gutenberg University [JGU], Medical University Graz, Centre de Recherche des Cordeliers [CRC (UMR_S_1138 / U1138)], Institut Pasteur d'Iran, Leibniz Institute of Plant Biochemistry [IPB], The University of Texas M.D. Anderson Cancer Center [Houston], Institut de pharmacologie moléculaire et cellulaire [IPMC], Lipides - Nutrition - Cancer [Dijon - U1231] [LNC], Centre méditerranéen de médecine moléculaire [C3M], Institut de Biologie Valrose [IBV], Petites Molécules de neuroprotection, neurorégénération et remyélinisation, Signalisation Hormonale, Physiopathologie Endocrinienne et Métabolique, Institut Cochin [IC UM3 (UMR 8104 / U1016)], Institut NeuroMyoGène [INMG], Paris-Centre de Recherche Cardiovasculaire [PARCC (UMR_S 970/ U970)], Marqueurs cardiovasculaires en situation de stress [MASCOT (UMR_S_942 / U942)], Institut de Recherche sur le Cancer et le Vieillissement [IRCAN], Centre de Recherche en Cancérologie de Marseille [CRCM], Centre for Integrative Biology - CBI [Inserm U964 - CNRS UMR7104 - IGBMC], Oncogenesis, Stress, Signaling [OSS], Institut Necker Enfants-Malades [INEM - UM 111 (UMR 8253 / U1151)], Institut de Biologie Intégrative de la Cellule [I2BC], Microbes, Intestin, Inflammation et Susceptibilité de l'Hôte [M2iSH], Centre de Recherches en Cancérologie de Toulouse [CRCT], Physiopathologie et traitement des maladies du foie, Centre d’Infection et d’Immunité de Lille - INSERM U 1019 - UMR 9017 - UMR 8204 [CIIL], Institut de Génétique et de Biologie Moléculaire et Cellulaire [IGBMC], Laboratoire Bio-PeroxIL. Biochimie du peroxysome, inflammation et métabolisme lipidique [Dijon] [BIO-PEROXIL], Centre de recherche sur l'Inflammation [CRI (UMR_S_1149 / ERL_8252 / U1149)], Unité de génétique et biologie des cancers [U830], Laboratoire d'Optique et Biosciences [LOB], Institut des Maladies Métaboliques et Casdiovasculaires [UPS/Inserm U1297 - I2MC], Différenciation et communication neuronale et neuroendocrine [DC2N], Institut de Recherche en Cancérologie de Montpellier [IRCM - U1194 Inserm - UM], Centre d'Immunologie de Marseille - Luminy [CIML], Physiopathologie et imagerie des troubles neurologiques [PhIND], Laboratory of Fundamental and Applied Bioenergetics = Laboratoire de bioénergétique fondamentale et appliquée [LBFA], Imagine - Institut des maladies génétiques (IHU) [Imagine - U1163], Institut Mondor de Recherche Biomédicale [IMRB], Franco-czech Laboratory for clinical research on obesity, University of Michigan [Ann Arbor], University of Michigan System, Institut de pharmacologie moléculaire et cellulaire (IPMC), Centre National de la Recherche Scientifique (CNRS)-Université Nice Sophia Antipolis (... - 2019) (UNS), COMUE Université Côte d'Azur (2015 - 2019) (COMUE UCA)-COMUE Université Côte d'Azur (2015 - 2019) (COMUE UCA)-Université Côte d'Azur (UCA), Lipides - Nutrition - Cancer [Dijon - U1231] (LNC), Université de Bourgogne (UB)-Institut National de la Santé et de la Recherche Médicale (INSERM)-AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement, Centre méditerranéen de médecine moléculaire (C3M), Université Nice Sophia Antipolis (... - 2019) (UNS), COMUE Université Côte d'Azur (2015 - 2019) (COMUE UCA)-COMUE Université Côte d'Azur (2015 - 2019) (COMUE UCA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Côte d'Azur (UCA), Institut de Biologie Valrose (IBV), COMUE Université Côte d'Azur (2015 - 2019) (COMUE UCA)-COMUE Université Côte d'Azur (2015 - 2019) (COMUE UCA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Côte d'Azur (UCA)-Centre National de la Recherche Scientifique (CNRS), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Paris-Sud - Paris 11 (UP11), Centre de Recherche des Cordeliers (CRC (UMR_S_1138 / U1138)), École pratique des hautes études (EPHE), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Sorbonne Université (SU)-Université de Paris (UP), Université Paris-Sud - Paris 11 (UP11)-Institut National de la Santé et de la Recherche Médicale (INSERM)-AP-HP Hôpital Bicêtre (Le Kremlin-Bicêtre), Nutrition, Métabolisme, Aquaculture (NuMéA), Université de Pau et des Pays de l'Adour (UPPA)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), Institut Cochin (IC UM3 (UMR 8104 / U1016)), Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université de Paris (UP), Institut NeuroMyoGène (INMG), Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM), Paris-Centre de Recherche Cardiovasculaire (PARCC - UMR-S U970), Hôpital Européen Georges Pompidou [APHP] (HEGP), Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Hôpitaux Universitaires Paris Ouest - Hôpitaux Universitaires Île de France Ouest (HUPO)-Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Hôpitaux Universitaires Paris Ouest - Hôpitaux Universitaires Île de France Ouest (HUPO)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Paris (UP), Institut de Recherche sur le Cancer et le Vieillissement (IRCAN), COMUE Université Côte d'Azur (2015 - 2019) (COMUE UCA)-COMUE Université Côte d'Azur (2015 - 2019) (COMUE UCA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université Côte d'Azur (UCA), Centre des Sciences du Goût et de l'Alimentation [Dijon] (CSGA), Université de Bourgogne (UB)-AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement-Centre National de la Recherche Scientifique (CNRS)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), Université Bourgogne Franche-Comté [COMUE] (UBFC), Centre de Recherche en Cancérologie de Marseille (CRCM), Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Institut Paoli-Calmettes, Fédération nationale des Centres de lutte contre le Cancer (FNCLCC)-Fédération nationale des Centres de lutte contre le Cancer (FNCLCC)-Aix Marseille Université (AMU), Centre for Integrative Biology - CBI (Inserm U964 - CNRS UMR7104 - IGBMC), Université de Strasbourg (UNISTRA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Institute of genetics and molecular and cellular biology-Centre National de la Recherche Scientifique (CNRS), Chemistry, Oncogenesis, Stress and Signaling (COSS), Université de Rennes 1 (UR1), Université de Rennes (UNIV-RENNES)-Université de Rennes (UNIV-RENNES)-CRLCC Eugène Marquis (CRLCC)-Institut National de la Santé et de la Recherche Médicale (INSERM), Institut Necker Enfants-Malades (INEM - UM 111 (UMR 8253 / U1151)), Unité de Nutrition Humaine (UNH), Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE)-Université Clermont Auvergne (UCA), Institut de Biologie Intégrative de la Cellule (I2BC), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS), Microbes, Intestin, Inflammation et Susceptibilité de l'Hôte (M2iSH), Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre de Recherche en Nutrition Humaine d'Auvergne (CRNH d'Auvergne)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE)-Université Clermont Auvergne (UCA), Institut des Maladies Neurodégénératives [Bordeaux] (IMN), Université de Bordeaux (UB)-Centre National de la Recherche Scientifique (CNRS), Centre International de Recherche en Infectiologie - UMR (CIRI), École normale supérieure - Lyon (ENS Lyon)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Centre de Recherches en Cancérologie de Toulouse (CRCT), Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Laboratoire de Physiologie et Génomique des Poissons (LPGP), Structure Fédérative de Recherche en Biologie et Santé de Rennes ( Biosit : Biologie - Santé - Innovation Technologique )-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), Hôpital Paul Brousse-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Paris-Saclay, Centre d’Infection et d’Immunité de Lille - INSERM U 1019 - UMR 9017 - UMR 8204 (CIIL), Institut Pasteur de Lille, Réseau International des Instituts Pasteur (RIIP)-Réseau International des Instituts Pasteur (RIIP)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Lille-Centre Hospitalier Régional Universitaire [Lille] (CHRU Lille)-Centre National de la Recherche Scientifique (CNRS), Institut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC), Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université de Strasbourg (UNISTRA), Laboratoire Bio-PeroxIL. Biochimie du peroxysome, inflammation et métabolisme lipidique [Dijon] (BIO-PEROXIL), Université de Bourgogne (UB)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Bourgogne Franche-Comté [COMUE] (UBFC), Centre de recherche sur l'Inflammation (CRI (UMR_S_1149 / ERL_8252 / U1149)), Institut Jean-Pierre Bourgin (IJPB), AgroParisTech-Université Paris-Saclay-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), Unité de génétique et biologie des cancers (U830), Institut Curie [Paris]-Institut National de la Santé et de la Recherche Médicale (INSERM), Laboratoire d'Optique et Biosciences (LOB), École polytechnique (X)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Institut des Maladies Métaboliques et Cardiovasculaires (I2MC), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Institut National de la Santé et de la Recherche Médicale (INSERM), Différenciation et communication neuronale et neuroendocrine (DC2N), Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU)-Institut National de la Santé et de la Recherche Médicale (INSERM), Institut de Recherche en Cancérologie de Montpellier (IRCM - U1194 Inserm - UM), CRLCC Val d'Aurelle - Paul Lamarque-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Montpellier (UM), Centre d'Immunologie de Marseille - Luminy (CIML), Aix Marseille Université (AMU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Physiopathologie et imagerie des troubles neurologiques (PhIND), Université de Caen Normandie (UNICAEN), Laboratory of Fundamental and Applied Bioenergetics = Laboratoire de bioénergétique fondamentale et appliquée (LBFA), Université Grenoble Alpes (UGA)-Institut National de la Santé et de la Recherche Médicale (INSERM), Epithelial biology and disease - Liliane Bettencourt Chair of Developmental Biology (Equipe Inserm U1163), Imagine - Institut des maladies génétiques (IHU) (Imagine - U1163), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Paris (UP)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Paris (UP), Biomécanique cellulaire et respiratoire (BCR), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Paris-Est Créteil Val-de-Marne - Paris 12 (UPEC UP12)-Centre National de la Recherche Scientifique (CNRS), Charles University [Prague]-Institut National de la Santé et de la Recherche Médicale (INSERM), This work was supported by the National Institute of General Medical Sciences [GM131919]., Université Paris-Sud - Paris 11 (UP11)-Institut National de la Santé et de la Recherche Médicale (INSERM), Marqueurs cardiovasculaires en situation de stress (MASCOT (UMR_S_942 / U942)), Institut National de la Santé et de la Recherche Médicale (INSERM)-Groupe Hospitalier Saint Louis - Lariboisière - Fernand Widal [Paris], Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Centre National de la Recherche Scientifique (CNRS)-Université de Paris (UP)-Université Sorbonne Paris Nord, Université de Strasbourg (UNISTRA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université de Strasbourg (UNISTRA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Physiopathologie des Adaptations Nutritionnelles (PhAN), Université de Nantes (UN)-Institut National de la Recherche Agronomique (INRA), Département Plateforme (PF I2BC), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS), Institut Gustave Roussy (IGR), Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Hôpitaux Universitaires Paris Ouest - Hôpitaux Universitaires Île de France Ouest (HUPO), Chinese Academy of Medical Sciences [Suzhou, Chine] (CAMS), Karolinska Institutet [Stockholm], Karolinska University Hospital [Stockholm], Department of Women's and Children's Health [Stockholm, Sweden], Centre National de la Recherche Scientifique (CNRS)-Centre Hospitalier Régional Universitaire [Lille] (CHRU Lille)-Université de Lille-Institut National de la Santé et de la Recherche Médicale (INSERM)-Institut Pasteur de Lille, Réseau International des Instituts Pasteur (RIIP)-Réseau International des Instituts Pasteur (RIIP), Université de Strasbourg (UNISTRA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-École polytechnique (X), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées, FHU OncoAge - Pathologies liées à l’âge [CHU Nice] (OncoAge), Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université Côte d'Azur (UCA)-Institut de Pharmacologie Moléculaire et Cellulaire [UNIV Côte d'Azur] (UPMC), Institut Universitaire du Cancer de Toulouse - Oncopole (IUCT Oncopole - UMR 1037), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-CHU Toulouse [Toulouse]-Institut National de la Santé et de la Recherche Médicale (INSERM), Life Sciences Institute [Ann Arbor, MI, USA], University of Michigan System-University of Michigan System, European Institute of Oncology IRCCS [Milan, Italy] (EIO), Ain Shams University (ASU), Johannes Gutenberg - Universität Mainz = Johannes Gutenberg University (JGU), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Sorbonne Université (SU)-Université Paris Cité (UPCité), Réseau International des Instituts Pasteur (RIIP), Leibniz Institute of Plant Biochemistry (IPB), Hebrew University of Jerusalem, Université Nice Sophia Antipolis (1965 - 2019) (UNS), COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-Centre National de la Recherche Scientifique (CNRS)-Université Côte d'Azur (UCA), Université de Bourgogne (UB)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Institut Agro Dijon, Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)-Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro), COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Côte d'Azur (UCA), COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université Côte d'Azur (UCA), Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université Paris Cité (UPCité), Paris-Centre de Recherche Cardiovasculaire (PARCC (UMR_S 970/ U970)), Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Hôpitaux Universitaires Paris Ouest - Hôpitaux Universitaires Île de France Ouest (HUPO)-Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Hôpitaux Universitaires Paris Ouest - Hôpitaux Universitaires Île de France Ouest (HUPO)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Paris Cité (UPCité), Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Centre National de la Recherche Scientifique (CNRS)-Université Paris Cité (UPCité)-Université Sorbonne Paris Nord, Aix Marseille Université (AMU)-Institut Paoli-Calmettes, Fédération nationale des Centres de lutte contre le Cancer (FNCLCC)-Fédération nationale des Centres de lutte contre le Cancer (FNCLCC)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Oncogenesis, Stress, Signaling (OSS), Institut des Maladies Métaboliques et Casdiovasculaires (UPS/Inserm U1297 - I2MC), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Grenoble Alpes (UGA), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Paris Cité (UPCité), Institut Mondor de Recherche Biomédicale (IMRB), Institut National de la Santé et de la Recherche Médicale (INSERM)-IFR10-Université Paris-Est Créteil Val-de-Marne - Paris 12 (UPEC UP12), Charles University [Prague] (CU)-Institut National de la Santé et de la Recherche Médicale (INSERM), Klionsky, D. J., Abdel-Aziz, A. K., Abdelfatah, S., Abdellatif, M., Abdoli, A., Abel, S., Abeliovich, H., Abildgaard, M. H., Abudu, Y. P., Acevedo-Arozena, A., Adamopoulos, I. E., Adeli, K., Adolph, T. E., Adornetto, A., Aflaki, E., Agam, G., Agarwal, A., Aggarwal, B. B., Agnello, M., Agostinis, P., Agrewala, J. N., Agrotis, A., Aguilar, P. V., Ahmad, S. T., Ahmed, Z. M., Ahumada-Castro, U., Aits, S., Aizawa, S., Akkoc, Y., Akoumianaki, T., Akpinar, H. A., Al-Abd, A. M., Al-Akra, L., Al-Gharaibeh, A., Alaoui-Jamali, M. A., Alberti, S., Alcocer-Gomez, E., Alessandri, C., Ali, M., Alim Al-Bari, M. A., Aliwaini, S., Alizadeh, J., Almacellas, E., Almasan, A., Alonso, A., Alonso, G. D., Altan-Bonnet, N., Altieri, D. C., Alvarez, E. M. C., Alves, S., Alves da Costa, C., Alzaharna, M. M., Amadio, M., Amantini, C., Amaral, C., Ambrosio, S., Amer, A. O., Ammanathan, V., An, Z., Andersen, S. U., Andrabi, S. A., Andrade-Silva, M., Andres, A. M., Angelini, S., Ann, D., Anozie, U. C., Ansari, M. Y., Antas, P., Antebi, A., Anton, Z., Anwar, T., Apetoh, L., Apostolova, N., Araki, T., Araki, Y., Arasaki, K., Araujo, W. L., Araya, J., Arden, C., Arevalo, M. -A., Arguelles, S., Arias, E., Arikkath, J., Arimoto, H., Ariosa, A. R., Armstrong-James, D., Arnaune-Pelloquin, L., Aroca, A., Arroyo, D. S., Arsov, I., Artero, R., Asaro, D. M. L., Aschner, M., Ashrafizadeh, M., Ashur-Fabian, O., Atanasov, A. G., Au, A. K., Auberger, P., Auner, H. W., Aurelian, L., Autelli, R., Avagliano, L., Avalos, Y., Aveic, S., Aveleira, C. A., Avin-Wittenberg, T., Aydin, Y., Ayton, S., Ayyadevara, S., Azzopardi, M., Baba, M., Backer, J. M., Backues, S. K., Bae, D. -H., Bae, O. -N., Bae, S. H., Baehrecke, E. H., Baek, A., Baek, S. -H., Baek, S. H., Bagetta, G., Bagniewska-Zadworna, A., Bai, H., Bai, J., Bai, X., Bai, Y., Bairagi, N., Baksi, S., Balbi, T., Baldari, C. T., Balduini, W., Ballabio, A., Ballester, M., Balazadeh, S., Balzan, R., Bandopadhyay, R., Banerjee, S., Banreti, A., Bao, Y., Baptista, M. S., Baracca, A., Barbati, C., Bargiela, A., Barila, D., Barlow, P. G., Barmada, S. J., Barreiro, E., Barreto, G. E., Bartek, J., Bartel, B., Bartolome, A., Barve, G. R., Basagoudanavar, S. H., Bassham, D. C., Bast, R. C., Basu, A., Batoko, H., Batten, I., Baulieu, E. E., Baumgarner, B. L., Bayry, J., Beale, R., Beau, I., Beaumatin, F., Bechara, L. R. G., Beck, G. R., Beers, M. F., Begun, J., Behrends, C., Behrens, G. M. N., Bei, R., Bejarano, E., Bel, S., Behl, C., Belaid, A., Belgareh-Touze, N., Bellarosa, C., Belleudi, F., Bello Perez, M., Bello-Morales, R., Beltran, J. S. D. O., Beltran, S., Benbrook, D. M., Bendorius, M., Benitez, B. A., Benito-Cuesta, I., Bensalem, J., Berchtold, M. W., Berezowska, S., Bergamaschi, D., Bergami, M., Bergmann, A., Berliocchi, L., Berlioz-Torrent, C., Bernard, A., Berthoux, L., Besirli, C. 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S., Steinkasserer, A., Stenmark, H., Sterneckert, J., Stevens, C., Stoka, V., Storch, S., Stork, B., Strappazzon, F., Strohecker, A. M., Stupack, D. G., Su, H., Su, L. -Y., Su, L., Suarez-Fontes, A. M., Subauste, C. S., Subbian, S., Subirada, P. V., Sudhandiran, G., Sue, C. M., Sui, X., Summers, C., Sun, G., Sun, J., Sun, K., Sun, M. -X., Sun, Q., Sun, Y., Sun, Z., Sunahara, K. K. S., Sundberg, E., Susztak, K., Sutovsky, P., Suzuki, H., Sweeney, G., Symons, J. D., Sze, S. C. W., Szewczyk, N. J., Tabecka-Lonczynska, A., Tabolacci, C., Tacke, F., Taegtmeyer, H., Tafani, M., Tagaya, M., Tai, H., Tait, S. W. G., Takahashi, Y., Takats, S., Talwar, P., Tam, C., Tam, S. Y., Tampellini, D., Tamura, A., Tan, C. T., Tan, E. -K., Tan, Y. -Q., Tanaka, M., Tang, D., Tang, J., Tang, T. -S., Tanida, I., Tao, Z., Taouis, M., Tatenhorst, L., Tavernarakis, N., Taylor, A., Taylor, G. A., Taylor, J. M., Tchetina, E., Tee, A. R., Tegeder, I., Teis, D., Teixeira, N., Teixeira-Clerc, F., Tekirdag, K. A., Tencomnao, T., Tenreiro, S., Tepikin, A. V., Testillano, P. S., Tettamanti, G., Tharaux, P. -L., Thedieck, K., Thekkinghat, A. A., Thellung, S., Thinwa, J. W., Thirumalaikumar, V. P., Thomas, S. M., Thomes, P. G., Thorburn, A., Thukral, L., Thum, T., Thumm, M., Tian, L., Tichy, A., Till, A., Timmerman, V., Titorenko, V. I., Todi, S. V., Todorova, K., Toivonen, J. M., Tomaipitinca, L., Tomar, D., Tomas-Zapico, C., Tomic, S., Tong, B. C. -K., Tong, C., Tong, X., Tooze, S. A., Torgersen, M. L., Torii, S., Torres-Lopez, L., Torriglia, A., Towers, C. G., Towns, R., Toyokuni, S., Trajkovic, V., Tramontano, D., Tran, Q. -G., Travassos, L. H., Trelford, C. B., Tremel, S., Trougakos, I. P., Tsao, B. P., Tschan, M. P., Tse, H. -F., Tse, T. F., Tsugawa, H., Tsvetkov, A. S., Tumbarello, D. A., Tumtas, Y., Tunon, M. J., Turcotte, S., Turk, B., Turk, V., Turner, B. J., Tuxworth, R. I., Tyler, J. K., Tyutereva, E. V., Uchiyama, Y., Ugun-Klusek, A., Uhlig, H. H., Ulamek-Koziol, M., Ulasov, I. V., Umekawa, M., Ungermann, C., Unno, R., Urbe, S., Uribe-Carretero, E., Ustun, S., Uversky, V. N., Vaccari, T., Vaccaro, M. I., Vahsen, B. F., Vakifahmetoglu-Norberg, H., Valdor, R., Valente, M. J., Valko, A., Vallee, R. B., Valverde, A. M., Van den Berghe, G., van der Veen, S., Van Kaer, L., van Loosdregt, J., van Wijk, S. J. L., Vandenberghe, W., Vanhorebeek, I., Vannier-Santos, M. A., Vannini, N., Vanrell, M. C., Vantaggiato, C., Varano, G., Varela-Nieto, I., Varga, M., Vasconcelos, M. H., Vats, S., Vavvas, D. G., Vega-Naredo, I., Vega-Rubin-de-Celis, S., Velasco, G., Velazquez, A. P., Vellai, T., Vellenga, E., Velotti, F., Verdier, M., Verginis, P., Vergne, I., Verkade, P., Verma, M., Verstreken, P., Vervliet, T., Vervoorts, J., Vessoni, A. T., Victor, V. M., Vidal, M., Vidoni, C., Vieira, O. V., Vierstra, R. D., Vigano, S., Vihinen, H., Vijayan, V., Vila, M., Vilar, M., Villalba, J. M., Villalobo, A., Villarejo-Zori, B., Villarroya, F., Villarroya, J., Vincent, O., Vindis, C., Viret, C., Viscomi, M. T., Visnjic, D., Vitale, I., Vocadlo, D. J., Voitsekhovskaja, O. V., Volonte, C., Volta, M., Vomero, M., Von Haefen, C., Vooijs, M. A., Voos, W., Vucicevic, L., Wade-Martins, R., Waguri, S., Waite, K. A., Wakatsuki, S., Walker, D. W., Walker, M. J., Walker, S. A., Walter, J., Wandosell, F. G., Wang, B., Wang, C. -Y., Wang, C., Wang, D., Wang, F., Wang, G., Wang, H., Wang, H. -G., Wang, J., Wang, K., Wang, L., Wang, M. H., Wang, M., Wang, N., Wang, P., Wang, Q. J., Wang, Q., Wang, Q. K., Wang, Q. A., Wang, W. -T., Wang, W., Wang, X., Wang, Y., Wang, Y. -Y., Wang, Z., Warnes, G., Warnsmann, V., Watada, H., Watanabe, E., Watchon, M., Wawrzynska, A., Weaver, T. E., Wegrzyn, G., Wehman, A. M., Wei, H., Wei, L., Wei, T., Wei, Y., Weiergraber, O. H., Weihl, C. C., Weindl, G., Weiskirchen, R., Wells, A., Wen, R. H., Wen, X., Werner, A., Weykopf, B., Wheatley, S. P., Whitton, J. L., Whitworth, A. J., Wiktorska, K., Wildenberg, M. E., Wileman, T., Wilkinson, S., Willbold, D., Williams, B., Williams, R. S. B., Williams, R. L., Williamson, P. R., Wilson, R. A., Winner, B., Winsor, N. J., Witkin, S. S., Wodrich, H., Woehlbier, U., Wollert, T., Wong, E., Wong, J. H., Wong, R. W., Wong, V. K. W., Wong, W. W. -L., Wu, A. -G., Wu, C., Wu, J., Wu, K. K., Wu, M., Wu, S. -Y., Wu, S., Wu, W. K. K., Wu, X., Wu, Y. -W., Wu, Y., Xavier, R. J., Xia, H., Xia, L., Xia, Z., Xiang, G., Xiang, J., Xiang, M., Xiang, W., Xiao, B., Xiao, G., Xiao, H., Xiao, H. -T., Xiao, J., Xiao, L., Xiao, S., Xiao, Y., Xie, B., Xie, C. -M., Xie, M., Xie, Y., Xie, Z., Xilouri, M., Xu, C., Xu, E., Xu, H., Xu, J., Xu, L., Xu, W. W., Xu, X., Xue, Y., Yakhine-Diop, S. M. S., Yamaguchi, M., Yamaguchi, O., Yamamoto, A., Yamashina, S., Yan, S., Yan, S. -J., Yan, Z., Yanagi, Y., Yang, C., Yang, D. -S., Yang, H., Yang, H. -T., Yang, J. -M., Yang, J., Yang, L., Yang, M., Yang, P. -M., Yang, Q., Yang, S., Yang, S. -F., Yang, W., Yang, W. Y., Yang, X., Yang, Y., Yao, H., Yao, S., Yao, X., Yao, Y. -G., Yao, Y. -M., Yasui, T., Yazdankhah, M., Yen, P. M., Yi, C., Yin, X. -M., Yin, Y., Yin, Z., Ying, M., Ying, Z., Yip, C. K., Yiu, S. P. T., Yoo, Y. H., Yoshida, K., Yoshii, S. R., Yoshimori, T., Yousefi, B., Yu, B., Yu, H., Yu, J., Yu, L., Yu, M. -L., Yu, S. -W., Yu, V. C., Yu, W. H., Yu, Z., Yuan, J., Yuan, L. -Q., Yuan, S., Yuan, S. -S. F., Yuan, Y., Yuan, Z., Yue, J., Yue, Z., Yun, J., Yung, R. L., Zacks, D. N., Zaffagnini, G., Zambelli, V. O., Zanella, I., Zang, Q. S., Zanivan, S., Zappavigna, S., Zaragoza, P., Zarbalis, K. S., Zarebkohan, A., Zarrouk, A., Zeitlin, S. O., Zeng, J., Zeng, J. -D., Zerovnik, E., Zhan, L., Zhang, B., Zhang, D. D., Zhang, H., Zhang, H. -L., Zhang, J., Zhang, J. -P., Zhang, K. Y. B., Zhang, L. W., Zhang, L., Zhang, M., Zhang, P., Zhang, S., Zhang, W., Zhang, X., Zhang, X. -W., Zhang, X. D., Zhang, Y., Zhang, Y. -D., Zhang, Y. -Y., Zhang, Z., Zhao, H., Zhao, L., Zhao, S., Zhao, T., Zhao, X. -F., Zhao, Y., Zheng, G., Zheng, K., Zheng, L., Zheng, S., Zheng, X. -L., Zheng, Y., Zheng, Z. -G., Zhivotovsky, B., Zhong, Q., Zhou, A., Zhou, B., Zhou, C., Zhou, G., Zhou, H., Zhou, J., Zhou, K., Zhou, R., Zhou, X. -J., Zhou, Y., Zhou, Z. -Y., Zhou, Z., Zhu, B., Zhu, C., Zhu, G. -Q., Zhu, H., Zhu, W. -G., Zhu, Y., Zhuang, H., Zhuang, X., Zientara-Rytter, K., Zimmermann, C. M., Ziviani, E., Zoladek, T., Zong, W. -X., Zorov, D. B., Zorzano, A., Zou, W., Zou, Z., Zuryn, S., Zwerschke, W., Brand-Saberi, B., Dong, X. C., Kenchappa, C. S., Lin, Y., Oshima, S., Rong, Y., Sluimer, J. C., Stallings, C. L., Tong, C. -K., and Centre National de la Recherche Scientifique (CNRS)
Subjects: 0301 basic medicine, Programmed cell death, Settore BIO/06, Autophagosome, Autolysosome, [SDV]Life Sciences [q-bio], lnfectious Diseases and Global Health Radboud Institute for Molecular Life Sciences [Radboudumc 4], Autophagy-Related Proteins, Review, Computational biology, [SDV.BC]Life Sciences [q-bio]/Cellular Biology, Biology, Settore MED/04, 03 medical and health sciences, stress, Chaperone-mediated autophagy, ddc:570, Autophagy, LC3, Animals, Humans, cancer, Settore BIO/10, flux, lysosome, macroautophagy, neurodegeneration, phagophore, vacuole, Set (psychology), Molecular Biology, 030102 biochemistry & molecular biology, business.industry, Interpretation (philosophy), Autophagosomes, Cell Biology, Multicellular organism, 030104 developmental biology, Knowledge base, Biological Assay, Lysosomes, business, Biomarkers, [SDV.MHEP]Life Sciences [q-bio]/Human health and pathology
Abstract: Contains fulltext : 232759.pdf (Publisher’s version ) (Closed access) In 2008, we published the first set of guidelines for standardizing research in autophagy. Since then, this topic has received increasing attention, and many scientists have entered the field. Our knowledge base and relevant new technologies have also been expanding. Thus, it is important to formulate on a regular basis updated guidelines for monitoring autophagy in different organisms. Despite numerous reviews, there continues to be confusion regarding acceptable methods to evaluate autophagy, especially in multicellular eukaryotes. Here, we present a set of guidelines for investigators to select and interpret methods to examine autophagy and related processes, and for reviewers to provide realistic and reasonable critiques of reports that are focused on these processes. These guidelines are not meant to be a dogmatic set of rules, because the appropriateness of any assay largely depends on the question being asked and the system being used. Moreover, no individual assay is perfect for every situation, calling for the use of multiple techniques to properly monitor autophagy in each experimental setting. Finally, several core components of the autophagy machinery have been implicated in distinct autophagic processes (canonical and noncanonical autophagy), implying that genetic approaches to block autophagy should rely on targeting two or more autophagy-related genes that ideally participate in distinct steps of the pathway. Along similar lines, because multiple proteins involved in autophagy also regulate other cellular pathways including apoptosis, not all of them can be used as a specific marker for bona fide autophagic responses. Here, we critically discuss current methods of assessing autophagy and the information they can, or cannot, provide. Our ultimate goal is to encourage intellectual and technical innovation in the field.
Published: 2021

5. Analysis of formin functions during cytokinesis using specific inhibitor SMIFH2

Author: Laining Zhang, Petro Smertenko, Dominik Novák, Natalia Moroz, Deirdre Fahy, Tetyana Smertenko, Nuria K. Koteyeva, Jozef Šamaj, John C. Sedbrook, Eduard Manoilov, Andrei Smertenko, Anna Kuchařová, Charitha Galva, and Alla S. Kostyukova
Subjects: 0106 biological sciences, Cytoplasm, Physiology, Arabidopsis, Formins, Plant Science, macromolecular substances, Phragmoplast, 01 natural sciences, Microtubules, Microtubule polymerization, 03 medical and health sciences, Microtubule, Tubulin, Tobacco, Genetics, Cytoskeleton, Uracil, News and Views, Actin, Research Articles, 030304 developmental biology, Cytokinesis, 0303 health sciences, biology, Chemistry, fungi, food and beverages, Thiones, Cell plate, Actins, Cell biology, biology.protein, 010606 plant biology & botany
Abstract: The phragmoplast separates daughter cells during cytokinesis by constructing the cell plate, which depends on interaction between cytoskeleton and membrane compartments. Proteins responsible for these interactions remain unknown, but formins can link cytoskeleton with membranes and several members of formin protein family localize to the cell plate. Progress in functional characterization of formins in cytokinesis is hindered by functional redundancies within the large formin gene family. We addressed this limitation by employing Small Molecular Inhibitor of Formin Homology 2 (SMIFH2), a small-molecule inhibitor of formins. Treatment of tobacco (Nicotiana tabacum) tissue culture cells with SMIFH2 perturbed localization of actin at the cell plate; slowed down both microtubule polymerization and phragmoplast expansion; diminished association of dynamin-related proteins with the cell plate independently of actin and microtubules; and caused cell plate swelling. Another impact of SMIFH2 was shortening of the END BINDING1b (EB1b) and EB1c comets on the growing microtubule plus ends in N. tabacum tissue culture cells and Arabidopsis thaliana cotyledon epidermis cells. The shape of the EB1 comets in the SMIFH2-treated cells resembled that of the knockdown mutant of plant Xenopus Microtubule-Associated protein of 215 kDa (XMAP215) homolog MICROTUBULE ORGANIZATION 1/GEMINI 1 (MOR1/GEM1). This outcome suggests that formins promote elongation of tubulin flares on the growing plus ends. Formins AtFH1 (A. thaliana Formin Homology 1) and AtFH8 can also interact with EB1. Besides cytokinesis, formins function in the mitotic spindle assembly and metaphase to anaphase transition. Our data suggest that during cytokinesis formins function in: (1) promoting microtubule polymerization; (2) nucleating F-actin at the cell plate; (3) retaining dynamin-related proteins at the cell plate; and (4) remodeling of the cell plate membrane.
Published: 2020

6. Impact of Wheat Streak Mosaic Virus on Peroxisome Proliferation, Redox Reactions, and Resistance Responses in Wheat

Author: Ivan Mishchenko, Yaroslav Fanin, Olga Molodchenkova, Alina Dunich, Lidiya Bezkrovna, Anna Dashchenko, Taras Nazarov, Andrei Smertenko, Olga Ryshchakova, Lidiya Mishchenko, and Ivan Motsnyi
Subjects: Chlorophyll, QH301-705.5, Viral pathogenesis, Peroxisome Proliferation, Peroxin, Context (language use), virus, Biology, Catalysis, Virus, Article, Inorganic Chemistry, Peroxisomes, peroxisome, Peroxisome fission, Biology (General), Physical and Theoretical Chemistry, QD1-999, Molecular Biology, Spectroscopy, Wheat streak mosaic virus, Triticum, Disease Resistance, Plant Diseases, redox homeostasis, Organic Chemistry, Chitinases, food and beverages, General Medicine, Glucan 1,3-beta-Glucosidase, Peroxisome, Potyviridae, biology.organism_classification, yield, Computer Science Applications, Cell biology, Plant Leaves, Chemistry, Phenotype, Peroxidases, WSMV, Reactive Oxygen Species, Oxidation-Reduction
Abstract: Although peroxisomes play an essential role in viral pathogenesis, and viruses are known to change peroxisome morphology, the role of genotype in the peroxisomal response to viruses remains poorly understood. Here, we analyzed the impact of wheat streak mosaic virus (WSMV) on the peroxisome proliferation in the context of pathogen response, redox homeostasis, and yield in two wheat cultivars, Patras and Pamir, in the field trials. We observed greater virus content and yield losses in Pamir than in Patras. Leaf chlorophyll and protein content measured at the beginning of flowering were also more sensitive to WSMV infection in Pamir. Patras responded to the WSMV infection by transcriptional up-regulation of the peroxisome fission genes PEROXIN 11C (PEX11C), DYNAMIN RELATED PROTEIN 5B (DRP5B), and FISSION1A (FIS1A), greater peroxisome abundance, and activation of pathogenesis-related proteins chitinase, and β-1,3-glucanase. Oppositely, in Pamir, WMSV infection suppressed transcription of peroxisome biogenesis genes and activity of chitinase and β-1,3-glucanase, and did not affect peroxisome abundance. Activity of ROS scavenging enzymes was higher in Patras than in Pamir. Thus, the impact of WMSV on peroxisome proliferation is genotype-specific and peroxisome abundance can be used as a proxy for the magnitude of plant immune response.
Published: 2021

7. Synthesis, antibacterial and antifungal activity of 1-[4-(1,1,3,3-tetramethylbutyl)phenoxy]-3-dialkylamino-2-propanol quaternary salts

Author: O. A. Smertenko, M. L. Dronova, Z. S. Suvorova, N. A. Vrynchanu, and Y. V. Korotkii
Subjects: chemistry.chemical_classification, biology, Aryl, Chemical structure, Epoxide, biology.organism_classification, Antimicrobial, Propanol, chemistry.chemical_compound, Minimum inhibitory concentration, chemistry, Organic chemistry, Candida albicans, Alkyl
Abstract: The emergence and spread of resistant strains of pathogens as well as reduction of the efficacy of current antimicrobial agents requires the development of novel antimicrobial compounds. The aim of the present study was synthesis and evaluation of antimicrobial activity of new arylaliphatic aminopropanols. The objects of the present study were 1-[4-(1,1,3,3-tetramethylbutyl)phenoxy]-3-dialkylamino-2-propanol quaternary salts (compounds I–XIV). Compounds synthesis was carried out by heating of precursor epoxide and excessive amount of appropriate amines in isopropanole, followed by treatment with excess of alkyl halides. Methods of elemental analysis, IR- and PMR-spectroscopy were used for confirmation of chemical structure. Antimicrobial activity against Staphylococcus аureus АTCC 25923, Escherichia coli ATCC 25922, Pseudomonas aeruginosa АТСС 27853 and Candida albicans NCTC 885/653 was determined by a broth dilution method and evaluated via minimum inhibitory concentration (MIC). Our investigation of antibacterial and antifungal activity of 1-[4-(1,1,3,3-tetra methylbutyl)phenoxy]-3-dialkylamino-2-propanol quaternary salts showed that compounds possess narrow spectrum, as well as broad spectrum action. Significant antimicrobial activity of the novel aryl aliphatic aminoalcohols indicates their potential usage as a component of new antimicrobial drugs.
Published: 2019

8. Phragmoplast expansion: the four-stroke engine that powers plant cytokinesis

Author: Andrei Smertenko
Subjects: 0301 basic medicine, Microtubule dynamics, Cell division, Cell plate assembly, Plant Science, Cell plate, Biology, Phragmoplast, Microtubules, Polymerization, Cell biology, 03 medical and health sciences, 030104 developmental biology, Microtubule, Plant Cells, Microtubule-Associated Proteins, Mitosis, Cytokinesis, Plant Proteins
Abstract: The phragmoplast is a plant-specific secretory module that partitions daughter cells during cytokinesis by constructing a cell plate from membranes and oligosaccharides. The cell plate is typically a long structure, which requires the phragmoplast to expand to complete cytokinesis. The phragmoplast expands by coordinating microtubule dynamics with membrane trafficking. Each step in phragmoplast expansion involves the establishment of anti-parallel microtubule overlaps that are enriched with the protein MAP65, which recruits cytokinetic vesicles through interaction with the tethering factor, TRAPPII. Cell plate assembly triggers dissolution of the anti-parallel overlaps and stabilization of microtubule plus ends through association with the cell plate assembly machinery. This opinion article discusses processes that drive phragmoplast expansion as well as highlights key questions that remain for better understanding its role in plant cell division.
Published: 2018

9. Phragmoplast navigator needs high IQ

Author: Andrei Smertenko
Subjects: 0106 biological sciences, 0301 basic medicine, Cell division, Polarity (physics), Arabidopsis Proteins, Arabidopsis, Plant Science, Biology, Cell division plane, Phragmoplast, 01 natural sciences, Cell biology, 03 medical and health sciences, 030104 developmental biology, Cell polarity, Cytokinesis, 010606 plant biology & botany
Abstract: Polarity cues direct tissue patterning by defining the cell division plane. Proteins containing the IQ67 calmodulin-binding domain govern cell division by establishing and maintaining cell polarity during cytokinesis.
Published: 2021

10. Apoptosis is not conserved in plants as revealed by critical examination of a model for plant apoptosis-like cell death

Author: Florentine Ballhaus, Peter V. Bozhkov, Andrei Smertenko, Vladimir Gogvadze, Adrian N. Dauphinee, and Elena A. Minina
Subjects: 0106 biological sciences, Programmed cell death, Necrosis, Physiology, QH301-705.5, Phagocytosis, Cell, Regulated cell death, Apoptosis, Plant Science, Stress, 01 natural sciences, General Biochemistry, Genetics and Molecular Biology, 03 medical and health sciences, Structural Biology, Plant Cells, medicine, Ferroptosis, Animals, Fragmentation (cell biology), Biology (General), Ecology, Evolution, Behavior and Systematics, Caspase, 030304 developmental biology, 2. Zero hunger, 0303 health sciences, biology, Cell Death, Botany, Cell Biology, Plants, Cell biology, medicine.anatomical_structure, Heat shock, Apoptosis-like programmed cell death, Caspases, biology.protein, Plasma membrane integrity, Protoplast shrinkage, medicine.symptom, General Agricultural and Biological Sciences, Mitochondrial dysfunction, Intracellular, Developmental Biology, Biotechnology, 010606 plant biology & botany, Research Article
Abstract: BackgroundAnimals and plants diverged over one billion years ago and evolved unique mechanisms for many cellular processes, including cell death. One of the most well-studied cell death programmes in animals, apoptosis, involves gradual cell dismantling and engulfment of cellular fragments, apoptotic bodies, through phagocytosis. However, rigid cell walls prevent plant cell fragmentation and thus apoptosis is not applicable for executing cell death in plants. Furthermore, plants are devoid of the key components of apoptotic machinery, including phagocytosis as well as caspases and Bcl-2 family proteins. Nevertheless, the concept of plant “apoptosis-like programmed cell death” (AL-PCD) is widespread. This is largely due to superficial morphological resemblances between plant cell death and apoptosis, and in particular between protoplast shrinkage in plant cells killed by various stimuli and animal cell volume decrease preceding fragmentation into apoptotic bodies.ResultsHere, we provide a comprehensive spatio-temporal analysis of cytological and biochemical events occurring in plant cells subjected to heat shock at 40–55 °C and 85 °C, the experimental conditions typically used to trigger AL-PCD and necrotic cell death, respectively. We show that cell death under both conditions was not accompanied by membrane blebbing or formation of apoptotic bodies, as would be expected during apoptosis. Instead, we observed instant and irreversible permeabilization of the plasma membrane and ATP depletion. These processes did not depend on mitochondrial functionality or the presence of Ca2+and could not be prevented by an inhibitor of ferroptosis. We further reveal that the lack of protoplast shrinkage at 85 °C, the only striking morphological difference between cell deaths induced by 40–55 °C or 85 °C heat shock, is a consequence of the fixative effect of the high temperature on intracellular contents.ConclusionsWe conclude that heat shock-induced cell death is an energy-independent process best matching definition of necrosis. Although the initial steps of this necrotic cell death could be genetically regulated, classifying it as apoptosis or AL-PCD is a terminological misnomer. Our work supports the viewpoint that apoptosis is not conserved across animal and plant kingdoms and demonstrates the importance of focusing on plant-specific aspects of cell death pathways.
Published: 2020

11. Classification and nomenclature of metacaspases and paracaspases: no more confusion with caspases

Author: Christiane Funk, Vanina E. Alvarez, Heinz D. Osiewacz, Juan José Cazzulo, Simon Stael, Boris Zhivotovsky, Chang Jae Choi, Frank Madeo, Jens Staal, Kailash C. Pandey, Lynn A. Megeney, Yigong Shi, Magali Casanova, Andrei Smertenko, Maurício F.M. Machado, Eric Lam, Renier A. L. van der Hoorn, Juergen Ruland, Ilana Berman-Frank, Panagiotis N. Moschou, Peter V. Bozhkov, Jeremy C. Mottram, Kay D. Bidle, Jerry Ståhlberg, Rudi Beyaert, Christopher M. Overall, Frédéric Bornancin, Kris Gevaert, Margot Thome, Assaf Vardi, Núria S. Coll, Patrick Gallois, Frank Van Breusegem, Thomas Nyström, Vishva M. Dixit, Marko Dolinar, Maria F. Suarez, Stephan Hailfinger, Nicolas Fasel, Emilio Gutierrez-Beltran, John A. Berges, Anna Linusson, Hannele Tuominen, Daniel Krappmann, Guy S. Salvesen, Marina Klemenčič, Elena A. Minina, Eugene V. Koonin, Canaan, Stephane, Swedish University of Agricultural Sciences (SLU), Universiteit Gent = Ghent University (UGENT), Universidad Nacional de San Martin (UNSAM), University of Wisconsin - Milwaukee, University of Haifa [Haifa], Rutgers, The State University of New Jersey [New Brunswick] (RU), Rutgers University System (Rutgers), Novartis Institutes for BioMedical Research (NIBR), Laboratoire d'ingénierie des systèmes macromoléculaires (LISM), Aix Marseille Université (AMU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), University of Texas at Austin [Austin], Centre for Research in Agricultural Genomics (CRAG), Genentech, Inc., Genentech, Inc. [San Francisco], University of Ljubljana, Université de Lausanne = University of Lausanne (UNIL), Umeå University, Universidade de Mogi das Cruces = University of Mogi das Cruzes (UMC), Karl-Franzens-Universität Graz, University of Ottawa [Ottawa], Institute of Molecular Biology and Biotechnology (IMBB-FORTH), Foundation for Research and Technology - Hellas (FORTH), University of York [York, UK], University of Gothenburg (GU), Goethe-University Frankfurt am Main, University of British Columbia (UBC), National Institute of Malaria Research [New Dehli, Inde] (NIMR), Indian Council of Medical Research [New Dehli] (ICMR), Technische Universität Munchen - Université Technique de Munich [Munich, Allemagne] (TUM), Sanford Burnham Prebys Medical Discovery Institute, Westlake University [Zhejiang], Washington State University (WSU), Universidad de Málaga [Málaga] = University of Málaga [Málaga], University of Oxford, Weizmann Institute of Science [Rehovot, Israël], Lomonosov Moscow State University (MSU), Knut and Alice Wallenberg Foundation, Swedish University of Agricultural Sciences and Linnean Center for Plant Biology, Universiteit Gent = Ghent University [Belgium] (UGENT), Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Aix Marseille Université (AMU), University of Lausanne (UNIL), Karl-Franzens-Universität [Graz, Autriche], University of Oxford [Oxford], University of Graz, and Technical University of Munich (TUM)
Subjects: Consensus, METACASPASES, Protein Conformation, [SDV]Life Sciences [q-bio], Computational biology, Article, purl.org/becyt/ford/1 [https], Structure-Activity Relationship, 03 medical and health sciences, 0302 clinical medicine, Terminology as Topic, medicine, Animals, Humans, CRYSTAL-STRUCTURE, purl.org/becyt/ford/1.6 [https], SPECIFICITY, Molecular Biology, Nomenclature, Caspase, PARACASPASES, ComputingMilieux_MISCELLANEOUS, Plant Proteins, 030304 developmental biology, Confusion, 0303 health sciences, biology, MALT1, Biology and Life Sciences, Cell Biology, 3. Good health, PROTEASES, [SDV] Life Sciences [q-bio], KEY, Mucosa-Associated Lymphoid Tissue Lymphoma Translocation 1 Protein, Caspases, biology.protein, CLAN CD, medicine.symptom, 030217 neurology & neurosurgery
Abstract: Metacaspases and paracaspases are proteases that were first identified as containing a caspase-like structural fold (Uren et al., 2000). Like caspases, metacaspases and paracaspases are multifunctional proteins regulating diverse biological phenomena, such as aging, immunity, proteostasis, and programmed cell death. The broad phylogenetic distribution of metacaspases and paracaspases across all kingdoms of life and large variation of their biochemical and structural features complicate classification and annotation of the rapidly growing number of identified homologs. Establishment of an adequate classification and unified nomenclature of metacaspases and paracaspases is especially important to avoid frequent confusion of these proteases with caspases—a tenacious misnomer that unfortunately does not appear to decline with time. This Letter represents a consensus opinion of researchers studying different aspects of caspases, metacaspases, and paracaspases in various organisms, ranging from microbes to plants and animals., This work was supported by the Knut and Alice Wallenberg Foundation.
Published: 2020

12. First report of bean yellow mosaic virus infecting Gladiolus sp. in Ukraine

Author: Hanna Korotieieva, Lidiya Mishchenko, Anna Dashchenko, Andrei Smertenko, Alina Dunich, and Roksolana Sovinska
Subjects: Gladiolus sp, biology, Botany, Plant Science, Bean yellow mosaic virus, biology.organism_classification
Published: 2020

13. The Arabidopsis R-SNARE VAMP714 is essential for polarization of PIN proteins in the establishment and maintenance of auxin gradients

Author: Jennifer F. Topping, Stuart A. Casson, Keith Lindsey, Kumari Fonseka, Patrick J. Hussey, Xiaoyan Gu, Andrei Smertenko, and Guangqin Guo
Subjects: chemistry.chemical_classification, biology, Chemistry, Endosome, Intercellular transport, Endocytic cycle, food and beverages, Signal transducing adaptor protein, Golgi apparatus, biology.organism_classification, Cell biology, symbols.namesake, Auxin, Arabidopsis, symbols, PIN proteins
Abstract: SummaryThe plant hormone auxin and its directional intercellular transport plays a major role in diverse aspects of plant growth and development. The establishment of auxin gradients in plants requires asymmetric distribution of members of the auxin efflux carrier PIN-FORMED (PIN) protein family to the plasma membrane. An endocytic pathway regulates the recycling of PIN proteins between the plasma membrane and endosomes, providing a mechanism for dynamic localization.N-ethylmaleimide-sensitive factor adaptor protein receptors (SNAP receptors, SNAREs) mediate fusion between vesicles and target membranes and are classed as Q- or R-SNAREs based on their sequence. We analysed gain- and loss-of-function mutants, dominant negative transgenics and protein localization of the Arabidopsis R-SNARE VAMP714 to understand its function.We demonstrate that VAMP714 is essential for the insertion of PINs into the plasmamembrane, for polar auxin transport, and for root gravitropism and morphogenesis.VAMP714gene expression is upregulated by auxin, and the VAMP714 protein co-localizes with ER and Golgi vesicles and with PIN proteins at the plasma membrane.It is proposed that VAMP714 mediates the delivery of PIN-carrying vesicles to the plasma membrane, and that this forms part of a positive regulatory loop in which auxin activates a VAMP714-dependent PIN/auxin transport system to control development.
Published: 2019

14. Phosphoinositides Break Microtubule Dynamics Symmetry in the Phragmoplast

Author: Mark Hubbard, Andrei Smertenko, and Washington State University (WSU)
Subjects: 0106 biological sciences, 0303 health sciences, Microtubule dynamics, [SDV]Life Sciences [q-bio], Cell Biology, Cell plate, Biology, Plants, Phragmoplast, Phosphatidylinositols, 01 natural sciences, Microtubules, Polymerization, 03 medical and health sciences, Microtubule, Biophysics, Cytokinesis, 030304 developmental biology, 010606 plant biology & botany
Abstract: Glucocorticoids (GCs) are widely used for the management of disease- or therapy-related complications in cancer patients. Recent data indicate that activation of GC receptors (GRs) precipitates breast cancer progression by favoring metastatic dissemination and cell survival at distant sites. These findings call for the re-evaluation of GC usage in patients with cancer.
Published: 2019

15. Differential Dynamic Changes of Reduced Trait Model for Analyzing the Plastic Response to Drought Phases: A Case Study in Spring Wheat

Author: Marwa N. M. E. Sanad, Andrei Smertenko, and Kimberley A. Garland-Campbell
Subjects: 0106 biological sciences, 0301 basic medicine, dynamic changes, media_common.quotation_subject, Drought tolerance, drought tolerance, Peroxisome Proliferation, Plant Science, lcsh:Plant culture, Biology, heritability, 01 natural sciences, Adaptability, adaptive mechanisms, 03 medical and health sciences, peroxisome proliferation, lcsh:SB1-1110, media_common, Original Research, Phenology, fungi, food and beverages, Adaptive response, Heritability, ROS homeostasis, 030104 developmental biology, spring wheat, Agronomy, Trait, Adaptive behavior (ecology), 010606 plant biology & botany
Abstract: Current limited water availability due to climate changes results in severe drought stress and desiccation in plants. Phenotyping drought tolerance remains challenging. In particular, our knowledge about the discriminating power of traits for capturing a plastic phenotype in high-throughput settings is scant. The study is designed to investigate the differential performance and broad-sense heritability of a battery set of morphological, physiological, and cellular traits to understand the adaptive phenotypic response to drought in spring wheat during the tillering stage. The potential of peroxisome abundance to predict the adaptive response under severe drought was assessed using a high-throughput technique for peroxisome quantification in plants. The research dissected the dynamic changes of some phenological traits during three successive phases of drought using two contrasting genotypes of adaptability to drought. The research demonstrates 5 main findings: (1) a reduction of the overall dimension of the phenological traits for robust phenotyping of the adaptive performance under drought; (2) the abundance of peroxisomes in response to drought correlate negatively with grain yield; (3) the efficiency of ROS homeostasis through peroxisome proliferation which seems to be genetically programmed; and (4) the dynamics of ROS homeostasis seems to be timing dependent mechanism, the tolerant genotype response is earlier than the susceptible genotype. This work will contribute to the identification of robust plastic phenotypic tools and the understanding of the mechanisms for adaptive behavior under drought conditions. Summary statement This study presents the estimated broad-sense heritability of 24 phenological traits under drought compared with non-stressed conditions. The results demonstrated a reduced model of the overall dimension of the phenological traits for phenotyping drought tolerant response including a novel trait (peroxisome abundance). Also, it displays that the adaptive mechanism through peroxisomes proliferation that is a genetic-dependent manner and related to the stress phase, since tolerant plants can sense the stress and maintain the cellular balance earlier than the sensitive plants.
Published: 2019
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16. Identification and characterization of the land-plant-specific microtubule nucleation factor MACET4

Author: Sharol Schmidt and Andrei Smertenko
Subjects: Centrosome, 0303 health sciences, biology, Arabidopsis Proteins, Arabidopsis, Cell Biology, Spindle Apparatus, Aster (cell biology), Phragmoplast, Microtubules, Microtubule polymerization, Cell biology, 03 medical and health sciences, 0302 clinical medicine, Tubulin, Microtubule, Agrobacterium tumefaciens, Preprophase band, Tobacco, biology.protein, Microtubule-Associated Proteins, 030217 neurology & neurosurgery, 030304 developmental biology, Microtubule nucleation
Abstract: Here, we show that the embryophyte (land-plant)-specific protein MACERATOR4 (MACET4) binds microtubules in vitro and in vivo, promotes microtubule polymerization at sub-critical tubulin concentrations, decreases the lag phase in microtubule bulk polymerization assays, and colocalizes with microtubule nucleation sites. Furthermore, we find that MACET4 forms oligomers that induce aster formation in vitro in a manner that is similar to aster formation mediated by centrosomes and TPX2. MACET4 is expressed during cell division and accumulates at the microtubule nucleation regions of the plant-specific cytokinetic microtubule array, the phragmoplast. We found that MACET4 localizes to the preprophase band and the cortical division zone, but not the spindle. MACET4 appears as cytoplasmic foci in vivo and forms octamers in vitro Transient expression in tobacco leaf pavement cells results in labeling of shrinking plus- and minus-ends. MACET4 facilitates microtubule depolymerization by increasing the frequency of catastrophes in vivo and by suppressing rescues in vitro Microtubules formed in the presence of MACET4 in vitro are shorter, most likely due to the depletion of the free tubulin pool. Accordingly, MACET4 knockdown results in longer phragmoplasts. We conclude that the direct activity of MACET4 is in promoting microtubule nucleation.This article has an associated First Person interview with the first author of the paper.
Published: 2019

17. Impact of heat and drought stress on peroxisome proliferation in quinoa

Author: Leonardo Hinojosa, Marwa N.M.E. Sanad, Patrick G. Steel, Kevin Murphy, David E. Jarvis, and Andrei Smertenko
Subjects: 0106 biological sciences, 0301 basic medicine, Crops, Agricultural, Stomatal conductance, Hot Temperature, Peroxisome Proliferation, Plant Science, Biology, Photosynthetic efficiency, 01 natural sciences, 03 medical and health sciences, Abundance (ecology), Gene Expression Regulation, Plant, Genetics, Peroxisomes, Chenopodium quinoa, Photosynthesis, Phylogeny, Abiotic stress, fungi, food and beverages, Cell Biology, Hydrogen Peroxide, Peroxisome, Arid, Droughts, 030104 developmental biology, Agronomy, Plant Stomata, Adaptation, Heat-Shock Response, 010606 plant biology & botany
Abstract: Although peroxisomes play a key role in plant metabolism under both normal and stressful growth conditions, the impact of drought and heat stress on the peroxisomes remains unknown. Quinoa represents an informative system for dissecting the impact of abiotic stress on peroxisome proliferation because it is adapted to marginal environments. Here we determined the correlation of peroxisome abundance with physiological responses and yield under heat, drought, and heat plus drought combination stresses in eight genotypes of quinoa. We found that all stresses caused a reduction in stomatal conductance and yield. Furthermore, H2O2 content increased under drought and heat plus drought. Principal component analysis demonstrated that peroxisome abundance correlated positively with H2O2 content in leaves and correlated negatively with yield. Person correlation coefficient for yield and peroxisome abundance (r=‐0.59) was higher than for commonly used photosynthetic efficiency (r=0.23), but comparable to those for classical stress indicators such as soil moisture content (r=0.51) or stomatal conductance (r=0.62). Our work established peroxisome abundance as a sensitive parameter for responses to heat and drought stress in the genetically diverse populations. As heat waves threaten agricultural productivity in arid climates, our findings will facilitate identification of genetic markers for improving yield of crops under extreme weather patterns.
Published: 2018

18. Epidermal expression of a sterol biosynthesis gene regulates root growth by a non-cell autonomous mechanism in Arabidopsis

Author: Naomi Cope-Selby, Jennifer F. Topping, Eleri Short, Gul Imriz, Patrick J. Hussey, Margaret Pullen, Dongbin Liu, Keith Lindsey, and Andrei Smertenko
Subjects: chemistry.chemical_classification, Auxin efflux, Pericycle, biology, chemistry, Auxin, Arabidopsis, Mutant, PIN1, Meristem, Signal transduction, biology.organism_classification, Cell biology
Abstract: The epidermis has been hypothesized to play a signalling role during plant development. One class of mutants showing defects in signal transduction and radial patterning are those in sterol biosynthesis. The expectation is that sterol biosynthesis is a constitutive cell-autonomous process for the maintenance of basic cellular functions. TheHYDRA1(HYD1) gene of Arabidopsis encodes an essential sterol Δ8-Δ7 isomerase, and althoughhyd1mutant seedlings are defective in radial patterning of several tissues, we show that theHYD1gene is expressed primarily in the root epidermis. Cell type-specific transgenic activation ofHYD1transcription reveals thatHYD1expression in the epidermis ofhyd1null mutants is sufficient to rescue root patterning and growth. Unexpectedly, expression ofHYD1in the vascular tissues and root meristem, though not endodermis or pericycle, also leads to phenotypic rescue. Phenotypic rescue is associated with rescued patterning of the PIN1 and PIN2 auxin efflux carriers. The importance of the epidermis is in part due to its role as a site for tissue-specific sterol biosynthesis, and auxin is a candidate for a non-cell autonomous signal.
Published: 2017
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19. Can Peroxisomes Inform Cellular Response to Drought?

Author: Andrei Smertenko
Subjects: 0106 biological sciences, 0301 basic medicine, Germplasm, Ecology, fungi, food and beverages, Plant Science, Computational biology, Peroxisome, Biology, Cellular level, 01 natural sciences, Phenotype, Droughts, 03 medical and health sciences, 030104 developmental biology, Abundance (ecology), Peroxisomes, Plant Physiological Phenomena, 010606 plant biology & botany
Abstract: Although plant germplasm contains numerous unknown traits for drought-tolerance, the ability to phenotype this material remains challenging. I propose that peroxisome abundance may be a viable parameter for the evaluation of drought response at the cellular level, and hence could be useful to improve phenotyping efforts.
Published: 2017

20. Extracellular Alkalinization as a Defense Response in Potato Cells

Author: Andrei Smertenko, Karen R. Fritch, Diwaker Tripathi, Natalia Moroz, Matthew J. Marcec, and Kiwamu Tanaka
Subjects: 0106 biological sciences, 0301 basic medicine, Plant Science, Colletotrichum coccodes, Plant disease resistance, 01 natural sciences, Microbiology, 03 medical and health sciences, Extracellular, Plant defense against herbivory, Bioassay, suspension cell culture, Verticillium dahliae, Pathogen, Original Research, apoplastic pH, biology, fungi, food and beverages, defense response, biology.organism_classification, extracellular alkalinization, 030104 developmental biology, Phytophthora infestans, potato, 010606 plant biology & botany
Abstract: A quantitative and robust bioassay to assess plant defense response is important for studies of disease resistance and also for the early identification of disease during pre- or non-symptomatic phases. An increase in extracellular pH is known to be an early defense response in plants. In this study, we propose a fast and reliable alkalinization assay to monitor plant defense response in potatoes. Using potato suspension cell cultures, we observed an alkalinization response against various pathogen- and plant-derived elicitors in a dose- and time-dependent manner. We also assessed the defense response against a variety of potato pathogens, such as protists (Phytophthora infestans and Spongospora subterranea) and fungi (Verticillium dahliae and Colletotrichum coccodes). Our results show that extracellular pH increases within 30 min in proportion to the number of pathogen spores added. Consistently with the alkalinization effect, the higher transcription level of several defense-related genes and production of reactive oxygen species was observed. Our results demonstrate that the alkalinization assay is an effective tool to study early stages of defense response in potatoes.
Published: 2017

21. Phragmoplast microtubule dynamics – a game of zones

Author: Sharol Schmidt, Matthew J. Marcec, Erika A. Serrano-Romero, Seanna Hewitt, Yan Liu, Lindani Moyo, Andrei Smertenko, Aaron J. Ogden, Rafal Kacprzyk, Hui Min Olivia Oung, and Caitlin N. Jacques
Subjects: 0301 basic medicine, education.field_of_study, Molecular Motor Proteins, Cell plate assembly, Population, Review, Cell Biology, Cell plate, Biology, Phragmoplast, Microtubules, Models, Biological, Polymerization, Cell biology, Microtubule polymerization, 03 medical and health sciences, 030104 developmental biology, Microtubule, Telophase, education, Cytokinesis, Signal Transduction
Abstract: Plant morphogenesis relies on the accurate positioning of the partition (cell plate) between dividing cells during cytokinesis. The cell plate is synthetized by a specialized structure called the phragmoplast, which consists of microtubules, actin filaments, membrane compartments and associated proteins. The phragmoplast forms between daughter nuclei during the transition from anaphase to telophase. As cells are commonly larger than the originally formed phragmoplast, the construction of the cell plate requires phragmoplast expansion. This expansion depends on microtubule polymerization at the phragmoplast forefront (leading zone) and loss at the back (lagging zone). Leading and lagging zones sandwich the ‘transition’ zone. A population of stable microtubules in the transition zone facilitates transport of building materials to the midzone where the cell plate assembly takes place. Whereas microtubules undergo dynamic instability in all zones, the overall balance appears to be shifted towards depolymerization in the lagging zone. Polymerization of microtubules behind the lagging zone has not been reported to date, suggesting that microtubule loss there is irreversible. In this Review, we discuss: (1) the regulation of microtubule dynamics in the phragmoplast zones during expansion; (2) mechanisms of the midzone establishment and initiation of cell plate biogenesis; and (3) signaling in the phragmoplast.
Published: 2017

22. Modeling hormonal control of cambium proliferation

Author: Vladyslav Oles, Andrei Smertenko, and Alexander Panchenko
Subjects: 0301 basic medicine, Cytokinins, Gene regulatory network, lcsh:Medicine, Plant Science, Biochemistry, Trees, chemistry.chemical_compound, Plant Tissues, Cell Signaling, Membrane Receptor Signaling, Plant Hormones, lcsh:Science, Plant Proteins, chemistry.chemical_classification, Multidisciplinary, Cambium, Plant Biochemistry, Plant Anatomy, food and beverages, Hormone Receptor Signaling, Signaling Cascades, Ethylene Signaling Cascade, Plant Physiology, Cytokinin, Vascular Bundles, Gibberellin, Stem cell, Research Article, Signal Transduction, Biology, Models, Biological, 03 medical and health sciences, Auxin, Xylem, Botany, Cell Proliferation, Indoleacetic Acids, fungi, lcsh:R, Biology and Life Sciences, Cell Biology, Gibberellins, Hormones, 030104 developmental biology, chemistry, Tree breeding, Auxins, lcsh:Q, Transcription Factors
Abstract: Rise of atmospheric CO2is one of the main causes of global warming. Catastrophic climate change can be avoided by reducing emissions and increasing sequestration of CO2. Trees are known to sequester CO2during photosynthesis, and then store it as wood biomass. Thus, breeding of trees with higher wood yield would mitigate global warming as well as augment production of renewable construction materials, energy, and industrial feedstock. Wood is made of cellulose-rich xylem cells produced through proliferation of a specialized stem cell niche called cambium. Importance of cambium in xylem cells production makes it an ideal target for the tree breeding programs; however our knowledge about control of cambium proliferation remains limited. The morphology and regulation of cambium differs from stem cell niches that control axial growth. For this reason, translating the knowledge about axial growth to radial growth has limited use. Furthermore, genetic approaches cannot be easily applied because overlaying tissues conceal cambium from direct observation and complicate identification of mutants. To overcome the paucity of experimental tools in cambium biology, we constructed a Boolean network CARENET (CAmbium Regulation gene NETwork) for modelling cambium activity, which includes the key transcription factors WOX4 and HD-ZIP III as well as their potential regulators. Our simulations revealed that: (1) auxin, cytokinin, gibberellin, and brassinosteroids act cooperatively in promoting transcription ofWOX4andHD-ZIP III; (2) auxin and cytokinin pathways negatively regulate each other; (3) hormonal pathways act redundantly in sustaining cambium activity; (4) individual cells in the stem cell niches can have diverse molecular identities. CARENET can be extended to include components of other signalling pathways and be integrated with models of xylem and phloem differentiation. Such extended models would facilitate breeding trees with higher wood yield.
Published: 2017

23. Plant Cytokinesis : Terminology for Structures and Processes

Author: Takashi Murata, Marisa S. Otegui, L. Andrew Staehelin, Magdalena Bezanilla, Daniël Van Damme, Andrei Smertenko, Farhah F. Assaad, Jozef Šamaj, Georgia Drakakaki, Sabine Müller, Marcel E. Janson, Viktor Žárský, Ian Moore, Yoshinobu Mineyuki, Lacey Samuels, Henrik Buschmann, Geoffrey O. Wasteneys, Marie-Theres Hauser, František Baluška, Carolyn G. Rasmussen, Emmanuel Panteris, and Anne-Catherine Schmit
Subjects: 0301 basic medicine, Cytoplasm, Microtubule-associated protein, Cell plate, Phragmoplast, Physcomitrella patens, Microtubules, Models, Biological, Chromosomes, Plant, 03 medical and health sciences, symbols.namesake, Division plane, Plant Cells, Terminology as Topic, Cytoskeleton, Cytokinesis, biology, fungi, Cell Membrane, food and beverages, Laboratorium voor Celbiologie, Cell Biology, Golgi apparatus, biology.organism_classification, Cell biology, Laboratory of Cell Biology, 030104 developmental biology, Preprophase band, symbols, EPS, Cell Division
Abstract: Plant cytokinesis is orchestrated by a specialized structure, the phragmoplast. The phragmoplast first occurred in representatives of Charophyte algae and then became the main division apparatus in land plants. Major cellular activities, including cytoskeletal dynamics, vesicle trafficking, membrane assembly, and cell wall biosynthesis, cooperate in the phragmoplast under the guidance of a complex signaling network. Furthermore, the phragmoplast combines plant-specific features with the conserved cytokinetic processes of animals, fungi, and protists. As such, the phragmoplast represents a useful system for understanding both plant cell dynamics and the evolution of cytokinesis. We recognize that future research and knowledge transfer into other fields would benefit from standardized terminology. Here, we propose such a lexicon of terminology for specific structures and processes associated with plant cytokinesis. A large number of phragmoplast proteins have been identified.Electron microscopy/tomography studies have produced nanoscale information about the architecture of phragmoplast and cell plate assembly stages in cryofixed cells.Novel components of the cortical division zone and cell plate fusion site have been discovered. This information lays a foundation for understanding how plant cells memorize the division plane throughout mitosis and how the cell plate is guided to its predetermined attachment site.MAP65 and plus end-directed kinesins contribute to the maintenance of the antiparallel overlap of phragmoplast microtubules. In addition, the MAP65-TRAPPII interaction plays a key role in cell plate assembly.Actin filaments align parallel to microtubules in the phragmoplast, while some microfilaments extend from cell plate margin to guide its expansion towards the fusion site.
Published: 2017

24. Autophagy and metacaspase determine the mode of cell death in plants

Author: Elena A. Minina, David E. Clapham, Kazutake Fukada, Maria F. Suarez, Geoffrey Daniel, Eugene I. Savenkov, Lada Filonova, Peter V. Bozhkov, Victoria Sanchez-Vera, Boris Zhivotovsky, Andrei Smertenko, and Vladimir Gogvadze
Subjects: Programmed cell death, Cell Death, biology, Autophagy, Cell, food and beverages, Cell Biology, Vacuole, Models, Biological, Metacaspase, Cell biology, medicine.anatomical_structure, Stress, Physiological, Apoptosis, Caspases, Report, biology.protein, medicine, Picea, Suspensor, Research Articles, Caspase, Plant Proteins
Abstract: Metacaspase-dependent autophagy in plants promotes cell disassembly during vacuolar cell death and inhibits necrosis., Although animals eliminate apoptotic cells using macrophages, plants use cell corpses throughout development and disassemble cells in a cell-autonomous manner by vacuolar cell death. During vacuolar cell death, lytic vacuoles gradually engulf and digest the cytoplasmic content. On the other hand, acute stress triggers an alternative cell death, necrosis, which is characterized by mitochondrial dysfunction, early rupture of the plasma membrane, and disordered cell disassembly. How both types of cell death are regulated remains obscure. In this paper, we show that vacuolar death in the embryo suspensor of Norway spruce requires autophagy. In turn, activation of autophagy lies downstream of metacaspase mcII-Pa, a key protease essential for suspensor cell death. Genetic suppression of the metacaspase–autophagy pathway induced a switch from vacuolar to necrotic death, resulting in failure of suspensor differentiation and embryonic arrest. Our results establish metacaspase-dependent autophagy as a bona fide mechanism that is responsible for cell disassembly during vacuolar cell death and for inhibition of necrosis.
Published: 2013

25. Late-Onset Sacsinopathy Diagnosed by Exome Sequencing and Comparative Genomic Hybridization

Author: Shona Bennett, Jennifer Duff, Tania Smertenko, Patrick Yu Wai Man, Patrick F. Chinnery, Helen Griffin, Angela Pyle, Mauro Santibanez-Koref, Rita Horvath, and Simon Zwolinski
Subjects: Adult, Male, congenital, hereditary, and neonatal diseases and abnormalities, Ataxia, Biology, Article, 03 medical and health sciences, Cellular and Molecular Neuroscience, 0302 clinical medicine, Genetics, medicine, Humans, Spinocerebellar Ataxias, Exome, Age of Onset, Heat-Shock Proteins, Exome sequencing, 030304 developmental biology, Comparative Genomic Hybridization, 0303 health sciences, Base Sequence, Genetic heterogeneity, Chromosome, Middle Aged, medicine.disease, Pedigree, Muscle Spasticity, Mutation, Mutation (genetic algorithm), Spinocerebellar ataxia, medicine.symptom, 030217 neurology & neurosurgery, Comparative genomic hybridization
Abstract: The molecular diagnosis of adult-onset autosomal recessive cerebellar ataxias remains challenging because of genetic heterogeneity. However, recently developed molecular genetic techniques will potentially revolutionize the diagnostic approach. Here we set out to define the genetic basis of the ataxia in two brothers with no molecular diagnosis. Clinical evaluation was followed by whole-exome second-generation sequencing and comparative genomic hybridization to determine the diagnosis. Whole-exome sequencing identified a hemizygous novel spastic ataxia of Charlevoix-Saguenay (SACS) stop-codon mutation in both brothers (c.13048G→T, p.E4350*) that was present in the mother, but not the father. Comparative genomic hybridization revealed a 0.7-Mb deletion on chromosome 13q12.12 in both brothers, which included SACS and was heterozygous in the asymptomatic father. The milder phenotype, caused by a whole-gene deletion and a stop-codon mutation in SACS, indicates a loss-of-function mechanism in late-onset autosomal recessive spastic ataxia of Charlevoix-Saguenay (ARSACS), and illustrates the importance of chromosomal rearrangements in the investigation of adult-onset ataxia.
Published: 2013

26. The Caspase-Related Protease Separase (EXTRA SPINDLE POLES) Regulates Cell Polarity and Cytokinesis inArabidopsis

Author: Eugene I. Savenkov, Andrei Smertenko, Panagiotis N. Moschou, Elena A. Minina, Peter V. Bozhkov, Patrick J. Hussey, Kazutake Fukada, and Stéphanie Robert
Subjects: Green Fluorescent Proteins, Immunoblotting, Arabidopsis, Coated vesicle, Plant Science, Isotropic cell growth, Microtubules, Plant Roots, Clathrin, Gene Expression Regulation, Plant, Cell polarity, Mitosis, Separase, Research Articles, Cytokinesis, Indoleacetic Acids, biology, Arabidopsis Proteins, Qa-SNARE Proteins, Reverse Transcriptase Polymerase Chain Reaction, Cell Membrane, Cell Polarity, Gene Expression Regulation, Developmental, Membrane Transport Proteins, Cell Biology, Cell plate, Plants, Genetically Modified, Cell biology, rab GTP-Binding Proteins, biology.protein, RNA Interference, Fluorescence Recovery After Photobleaching, Protein Binding
Abstract: Vesicle trafficking plays an important role in cell division, establishment of cell polarity, and translation of environmental cues to developmental responses. However, the molecular mechanisms regulating vesicle trafficking remain poorly understood. Here, we report that the evolutionarily conserved caspase-related protease separase (EXTRA SPINDLE POLES [ESP]) is required for the establishment of cell polarity and cytokinesis in Arabidopsis thaliana. At the cellular level, separase colocalizes with microtubules and RabA2a (for RAS GENES FROM RAT BRAINA2a) GTPase-positive structures. Separase facilitates polar targeting of the auxin efflux carrier PIN-FORMED2 (PIN2) to the rootward side of the root cortex cells. Plants with the radially swollen4 (rsw4) allele with compromised separase activity, in addition to mitotic failure, display isotropic cell growth, perturbation of auxin gradient formation, slower gravitropic response in roots, and cytokinetic failure. Measurements of the dynamics of vesicle markers on the cell plate revealed an overall reduction of the delivery rates of KNOLLE and RabA2a GTPase in separase-deficient roots. Furthermore, dissociation of the clathrin light chain, a protein that plays major role in the formation of coated vesicles, was slower in rsw4 than in the control. Our results demonstrate that separase is a key regulator of vesicle trafficking, which is indispensable for cytokinesis and the establishment of cell polarity.
Published: 2013

27. Impact of salt stress, cell death, and autophagy on peroxisomes: quantitative and morphological analyses using small fluorescent probe N-BODIPY

Author: Deirdre Fahy, Kerstin Duscha, Madison Lyons, Peter V. Bozhkov, Andrei Smertenko, Fuquan Liu, H. Ekkehard Neuhaus, Jianping Hu, Hans-Henning Kunz, Patrick G. Steel, and Marwa N.M.E. Sanad
Subjects: 0106 biological sciences, 0301 basic medicine, Boron Compounds, Programmed cell death, ATG5, Arabidopsis, Peroxisome Proliferation, plant, Apoptosis, Sodium Chloride, 01 natural sciences, 03 medical and health sciences, stress, Stress, Physiological, Peroxisomes, peroxisome, N-BODIPY, Fluorescent Dyes, chemistry.chemical_classification, Reactive oxygen species, Multidisciplinary, biology, Staining and Labeling, Autophagy, Cell Biology, Peroxisome, biology.organism_classification, Nitro Compounds, Corrigenda, Cell biology, 030104 developmental biology, chemistry, Biochemistry, Photorespiration, 010606 plant biology & botany
Abstract: Plant peroxisomes maintain a plethora of key life processes including fatty acid β-oxidation, photorespiration, synthesis of hormones, and homeostasis of reactive oxygen species (ROS). Abundance of peroxisomes in cells is dynamic; however mechanisms controlling peroxisome proliferation remain poorly understood because measuring peroxisome abundance is technically challenging. Counting peroxisomes in individual cells of complex organs by electron or fluorescence microscopy is expensive and time consuming. Here we present a simple technique for quantifying peroxisome abundance using the small probe Nitro-BODIPY, which in vivo fluoresces selectively inside peroxisomes. The physiological relevance of our technique was demonstrated using salinity as a known inducer of peroxisome proliferation. While significant peroxisome proliferation was observed in wild-type Arabidopsis leaves following 5-hour exposure to NaCl, no proliferation was detected in the salt-susceptible mutants fry1-6, sos1-14, and sos1-15. We also found that N-BODIPY detects aggregation of peroxisomes during final stages of programmed cell death and can be used as a marker of this stage. Furthermore, accumulation of peroxisomes in an autophagy-deficient Arabidopsis mutant atg5 correlated with N-BODIPY labeling. In conclusion, the technique reported here enables quantification of peroxisomes in plant material at various physiological settings. Its potential applications encompass identification of genes controlling peroxisome homeostasis and capturing stress-tolerant genotypes.
Published: 2016

28. EXTRA SPINDLE POLES (Separase) controls anisotropic cell expansion in Norway spruce (Picea abies) embryos independently of its role in anaphase progression

Author: Patrick J. Hussey, Eugene I. Savenkov, Emilio Gutierrez-Beltran, Elena A. Minina, Kazutake Fukada, Peter V. Bozhkov, Panagiotis N. Moschou, Andrei Smertenko, Maria F. Suarez, Salim Hossain Reza, Victoria Sanchez-Vera, Knut and Alice Wallenberg Foundation, Olle Engkvist Foundation, The Erling-Persson Family Foundation, August Teodor Larsson Foundation, Swedish Research Council, Swedish Foundation for Strategic Research, and Ministerio de Ciencia e Innovación (España)
Subjects: 0301 basic medicine, Physiology, Plant Science, Biology, Cell cycle, Phragmoplast, Microtubules, Chromosomes, Plant, 03 medical and health sciences, fluids and secretions, Gene Expression Regulation, Plant, Sequence Analysis, Protein, Amino Acid Sequence, Cloning, Molecular, Picea, Metaphase, Mitosis, Phylogeny, Separase, Anaphase, Cell Proliferation, Cytokinesis, Plant Proteins, Genetics, Kinetochore, Spindle midzone, Gene Expression Regulation, Developmental, Proteases, biochemical phenomena, metabolism, and nutrition, Cell biology, Spruce (Picea abies), Protein Transport, 030104 developmental biology, Gene Knockdown Techniques, Embryogenesis, Seeds, Anisotropy
Abstract: The caspase‐related protease separase (EXTRA SPINDLE POLES, ESP) plays a major role in chromatid disjunction and cell expansion in Arabidopsis thaliana. Whether the expansion phenotypes are linked to defects in cell division in Arabidopsis ESP mutants remains elusive. Here we present the identification, cloning and characterization of the gymnosperm Norway spruce (Picea abies, Pa) ESP. We used the P. abies somatic embryo system and a combination of reverse genetics and microscopy to explore the roles of Pa ESP during embryogenesis. Pa ESP was expressed in the proliferating embryonal mass, while it was absent in the suspensor cells. Pa ESP associated with kinetochore microtubules in metaphase and then with anaphase spindle midzone. During cytokinesis, it localized on the phragmoplast microtubules and on the cell plate. Pa ESP deficiency perturbed anisotropic expansion and reduced mitotic divisions in cotyledonary embryos. Furthermore, whilst Pa ESP can rescue the chromatid nondisjunction phenotype of Arabidopsis ESP mutants, it cannot rescue anisotropic cell expansion. Our data demonstrate that the roles of ESP in daughter chromatid separation and cell expansion are conserved between gymnosperms and angiosperms. However, the mechanisms of ESP‐mediated regulation of cell expansion seem to be lineage‐specific., This work was supported by grants from the VR Swedish Research Council (to P.N.M. and P.V.B.), Pehrssons Fund (to P.V.B.), the Swedish Foundation for Strategic Research (to P.V.B.), the Olle Engkvist Foundation (to P.V.B.), the Knut and Alice Wallenberg Foundation (to P.V.B.), the August T. Larsson Foundation (to A.P.S. and P.V.B.), Hatch Grant WNP00826 (to A.P.S.), and a Spanish Ministry of Science and Innovation grant (AGL2010‐15684 to M.F.S). V.S‐V. was recipient of a FPI fellowship from the Spanish Ministry of Science and Innovation (BES‐2008‐003592).
Published: 2016

29. Separase Promotes Microtubule Polymerization by Activating CENP-E-Related Kinesin Kin7

Author: Peter V. Bozhkov, Andrei Smertenko, Panagiotis N. Moschou, Emilio Gutierrez-Beltran, Swedish Research Council, Knut and Alice Wallenberg Foundation, Swedish Foundation for Strategic Research, National Institute of Food and Agriculture (US), August Teodor Larsson Foundation, Olle Engkvist Foundation, and The Erling-Persson Family Foundation
Subjects: 0301 basic medicine, Chromosomal Proteins, Non-Histone, Protein domain, Arabidopsis, Kinesins, Plasma protein binding, Biology, Microtubules, General Biochemistry, Genetics and Molecular Biology, Microtubule polymerization, Polymerization, 03 medical and health sciences, Gravitropism, Protein Domains, Microtubule, Cell polarity, Homologous chromosome, Morphogenesis, Molecular Biology, Separase, Sequence Homology, Amino Acid, Arabidopsis Proteins, Temperature, Cell Polarity, Cell Biology, Cell biology, Enzymes, 030104 developmental biology, Multiprotein Complexes, Proteolysis, Biocatalysis, Kinesin, Cell Nucleus Division, Developmental Biology, Protein Binding
Abstract: Microtubules play an essential role in breaking cellular symmetry. We have previously shown that separase associates with microtubules and regulates microtubule-dependent establishment of cell polarity in Arabidopsis. However, separase lacks microtubule-binding activity, raising questions about mechanisms underlying this phenomenon. Here we report that the N-terminal non-catalytic domain of separase binds to the C-terminal tail domain of three homologs of the centromeric protein CENP-E Kinesin 7 (Kin7). Conformational changes of Kin7 induced upon binding to separase facilitate recruitment of Kin7/separase complex (KISC) onto microtubules. KISC operates independently of proteolytic activity of separase in promoting microtubule rescue and pauses, as well as in suppressing catastrophes. Genetic complementation experiments in conditional separase mutant rsw4 background demonstrate the importance of KISC for the establishment of cell polarity and for plant development. Our study establishes a mechanism governing microtubule dynamics via the separase-dependent activation of CENP-E-related kinesins., This work was supported by grants from the Swedish Research Council (to P.N.M. and P.V.B.), Knut and Alice Wallenberg Foundation (to P.V.B.), the Swedish Foundation for Strategic Research (to P.V.B.), August T. Larsson Foundation (to A.S. and P.V.B.), Olle Engkvist Foundation (to P.V.B.), Pehrssons Fund (to P.V.B.), and NIFA hatch project WNP00826 (to A.S.).
Published: 2016

30. Morphological classification of plant cell deaths

Author: Eric Lam, Peter V. Bozhkov, T J Wolpert, Ernst J. Woltering, Andrei Smertenko, Boris Zhivotovsky, Michael Taliansky, Luis A. J. Mur, Vernonica E. Franklin-Tong, F. Van Breusegem, John Mundy, Alan M. Jones, Eric P. Beers, Morten Petersen, Maki Kawai-Yamada, Patrick Gallois, Jeffery L. Dangl, W.G. van Doorn, and Ikuko Hara-Nishimura
Subjects: Hypersensitive response, autophagy, Programmed cell death, hypersensitive response, senescence, Necrosis, contributes, Leerstoelgroep Tuinbouwproductieketens, Review, Vacuole, Biology, self-incompatibility, Plant Cells, otorhinolaryngologic diseases, medicine, Animals, Molecular Biology, Plant Physiological Phenomena, Horticultural Supply Chains, mechanisms, xylogenesis, Innate immune system, Cell Death, AFSG Quality in Chains, Cell growth, fungi, Neurodegeneration, apoptosis, food and beverages, Cell Biology, Plants, PE&RC, medicine.disease, Cell biology, arabidopsis, Apoptosis, Vacuoles, medicine.symptom, innate immune-response
Abstract: Programmed cell death (PCD) is an integral part of plant development and of responses to abiotic stress or pathogens. Although the morphology of plant PCD is, in some cases, well characterised and molecular mechanisms controlling plant PCD are beginning to emerge, there is still confusion about the classification of PCD in plants. Here we suggest a classification based on morphological criteria. According to this classification, the use of the term 'apoptosis' is not justified in plants, but at least two classes of PCD can be distinguished: vacuolar cell death and necrosis. During vacuolar cell death, the cell contents are removed by a combination of autophagy-like process and release of hydrolases from collapsed lytic vacuoles. Necrosis is characterised by early rupture of the plasma membrane, shrinkage of the protoplast and absence of vacuolar cell death features. Vacuolar cell death is common during tissue and organ formation and elimination, whereas necrosis is typically found under abiotic stress. Some examples of plant PCD cannot be ascribed to either major class and are therefore classified as separate modalities. These are PCD associated with the hypersensitive response to biotrophic pathogens, which can express features of both necrosis and vacuolar cell death, PCD in starchy cereal endosperm and during self-incompatibility. The present classification is not static, but will be subject to further revision, especially when specific biochemical pathways are better defined.
Published: 2011

31. Strategies of actin reorganisation in plant cells

Author: Andrei Smertenko, Michael J. Deeks, and Patrick J. Hussey
Subjects: biology, Arabidopsis, Arp2/3 complex, Actin remodeling, macromolecular substances, Cell Biology, Cofilin, Filamin, Actins, Cell Line, Cell biology, Actin Cytoskeleton, Actin remodeling of neurons, Treadmilling, biology.protein, MDia1, Cytoskeleton
Abstract: Spatial-temporal flexibility of the actin filament network (F-actin) is essential for all basic cellular functions and is governed by a stochastic dynamic model. In this model, actin filaments that randomly polymerise from a pool of free actin are bundled with other filaments and severed by ADF/cofilin. The fate of the severed fragments is not known. It has been proposed that the fragments are disassembled and the monomeric actin recycled for the polymerisation of new filaments. Here, we have generated tobacco cell lines and Arabidopsis plants expressing the actin marker Lifeact to address the mechanisms of F-actin reorganisation in vivo. We found that F-actin is more dynamic in isotropically expanding cells and that the density of the network changes with a periodicity of 70 seconds. The depolymerisation rate, but not the polymerisation rate, of F-actin increases when microtubules are destabilised. New filaments can be assembled from shorter free cytoplasmic fragments, from the products of F-actin severing and by polymerisation from the ends of extant filaments. Thus, remodelling of F-actin might not require bulk depolymerisation of the entire network, but could occur via severing and end-joining of existing polymers.
Published: 2010

32. The plant formin AtFH4 interacts with both actin and microtubules, and contains a newly identified microtubule-binding domain

Author: Patrick J. Hussey, Matyáš Fendrych, Andrei Smertenko, Viktor Žárský, Kenneth S. Bell, Fatima Cvrčková, Karl Oparka, and Michael J. Deeks
Subjects: Recombinant Fusion Proteins, Green Fluorescent Proteins, Arabidopsis, Formins, macromolecular substances, Biology, Endoplasmic Reticulum, Microtubules, Microtubule, Cytoskeleton, Arabidopsis Proteins, Endoplasmic reticulum, Microfilament Proteins, fungi, food and beverages, Cell Biology, Microfilament Protein, Actin cytoskeleton, Actins, Protein Structure, Tertiary, Cell biology, biology.protein, MDia1, Protein Binding, Binding domain
Abstract: The dynamic behaviour of the actin cytoskeleton in plants relies on the coordinated action of several classes of actin-binding proteins (ABPs). These ABPs include the plant-specific subfamilies of actin-nucleating formin proteins. The model plant species Arabidopsis thaliana has over 20 formin proteins, all of which contain plant-specific regions in place of the GTPase-binding domain, formin homology (FH)3 domain, and DAD and DID motifs found in many fungal and animal formins. We have identified for the first time a plant-specific region of the membrane-integrated formin AtFH4 that mediates an association with the microtubule cytoskeleton. In vitro analysis shows that this region (named the GOE domain) binds directly to microtubules. Overexpressed AtFH4 accumulates at the endoplasmic reticulum membrane and co-aligns the endoplasmic reticulum with microtubules. The FH1 and FH2 domains of formins are conserved in plants, and we show that these domains of AtFH4 nucleate F-actin. Together, these data suggest that the combination of plant-specific and conserved domains enables AtFH4 to function as an interface between membranes and both major cytoskeletal networks.
Published: 2010

33. Sugar transporters of the major facilitator superfamily in aphids; from gene prediction to functional characterization

Author: John A. Gatehouse, Andrei Smertenko, Shuji Shigenobu, Angela E. Douglas, Daniel R. G. Price, Calum W. Russell, K. Tibbles, Angharad M. R. Gatehouse, and Elaine Fitches
Subjects: Expressed sequence tag, Gene prediction, food and beverages, Fructose, Biology, Genome, Major facilitator superfamily, chemistry.chemical_compound, chemistry, Biochemistry, Insect Science, Genetics, Sugar transporter, Sugar, Molecular Biology, Gene
Abstract: Analysis of the pea aphid (Acyrthosiphon pisum) genome using signatures specific to the Major Facilitator Superfamily (Pfam Clan CL0015) and the Sugar_tr family (Pfam Family PF00083) has identified 54 genes encoding potential sugar transporters, of which 38 have corresponding ESTs. Twenty-nine genes contain the InterPro IPR003663 hexose transporter signature. The protein encoded by Ap_ST3, the most abundantly expressed sugar transporter gene, was functionally characterized by expression as a recombinant protein. Ap_ST3 acts as a low-affinity uniporter for fructose and glucose that does not depend on Na(+) or H(+) for activity. Ap_ST3 was expressed at elevated levels in distal gut tissue, consistent with a role in gut sugar transport. The A. pisum genome shows evidence of duplications of sugar transporter genes.
Published: 2010

34. BODIPY probes to study peroxisome dynamics in vivo

Author: Marie Landrum, Patrick G. Steel, Patrick J. Hussey, Robert Edwards, and Andrei Smertenko
Subjects: chemistry.chemical_classification, Biomolecule, Cell Biology, Plant Science, Biology, Peroxisome, Plant cell, Fluorescence, chemistry.chemical_compound, chemistry, Biochemistry, In vivo, Genetics, Biophysics, Molecule, BODIPY, Function (biology)
Abstract: There is a continuing need for bioprobes that are target-specific and combine speed of delivery with maintenance of normal cell behaviour. Towards this end, we are developing small pro-fluorescent molecules that provide such specificity through chemical activation by biomolecules. We have generated a set of BODIPY (boron dipyrromethane) fluorophores, including one that is intrinsically non-fluorescent but on incubation with cells becomes fluorescent at its target site. Addition of these BODIPY probes to plant cells identifies peroxisomes, as verified by co-localization with an SKL-FP construct. Interestingly, in mammalian cells, co-localization with the mammalian peroxisomal marker SelectFX(TM) was not observed. These data suggest fundamental differences in peroxisome composition, development or function between plant and animal cells.
Published: 2010

35. ArabidopsisRab-E GTPases exhibit a novel interaction with a plasma-membrane phosphatidylinositol-4-phosphate 5-kinase

Author: Ian Moore, Luísa Camacho, Andrei Smertenko, Patrick J. Hussey, and José Pérez-Gómez
Subjects: Phosphatidylinositol 4-phosphate, GTPase, symbols.namesake, chemistry.chemical_compound, Two-Hybrid System Techniques, Arabidopsis, Tobacco, Point Mutation, Secretion, Kinase activity, biology, Arabidopsis Proteins, Endoplasmic reticulum, Cell Membrane, fungi, Cell Biology, Golgi apparatus, Plants, Genetically Modified, biology.organism_classification, Cell biology, Plant Leaves, Phosphotransferases (Alcohol Group Acceptor), Biochemistry, chemistry, rab GTP-Binding Proteins, symbols, Rab, Protein Binding
Abstract: Rab GTPases of the Arabidopsis Rab-E subclass are related to mammalian Rab8 and are implicated in membrane trafficking from the Golgi to the plasma membrane. Using a yeast two-hybrid assay, Arabidopsis phosphatidylinositol-4-phosphate 5-kinase 2 (PtdIns(4)P 5-kinase 2; also known as PIP5K2), was shown to interact with all five members of the Rab-E subclass but not with other Rab subclasses residing at the Golgi or trans-Golgi network. Interactions in yeast and in vitro were strongest with RAB-E1d[Q74L] and weakest with the RAB-E1d[S29N] suggesting that PIP5K2 interacts with the GTP-bound form. PIP5K2 exhibited kinase activity towards phosphatidylinositol phosphates with a free 5-hydroxyl group, consistent with PtdIns(4)P 5-kinase activity and this activity was stimulated by Rab binding. Rab-E proteins interacted with PIP5K2 via its membrane occupancy and recognition nexus (MORN) domain which is missing from animal and fungal PtdIns(4)P 5-kinases. In plant cells, GFP:PIP5K2 accumulated at the plasma membrane and caused YFP:RAB-E1d to relocate there from its usual position at the Golgi. GFP:PIP5K2 was rapidly turned over by proteasomal activity in planta, and overexpression of YFP:PIP5K2 caused pleiotropic growth abnormalities in transgenic Arabidopsis. We propose that plant cells exhibit a novel interaction in which PIP5K2 binds GTP-bound Rab-E proteins, which may stimulate temporally or spatially localized PtdIns(4,5)P2 production at the plasma membrane.
Published: 2009

36. Actin-Depolymerizing Factor2-Mediated Actin Dynamics Are Essential for Root-Knot Nematode Infection ofArabidopsis

Author: Pierre Abad, Mathilde Clément, Tijs Ketelaar, Mohamed Youssef Banora, Gilbert Engler, Janice de Almeida Engler, Patrick J. Hussey, Andrei Smertenko, Natalia Rodiuc, Interactions Biotiques et Santé Végétale, Institut National de la Recherche Agronomique (INRA), Wageningen University and Research Centre (WUR), School of Biological and Biomedical Sciences, and Durham University
Subjects: 0106 biological sciences, Arabidopsis, Plant Science, Giant Cells, Plant Roots, in-vivo, 01 natural sciences, Gene Expression Regulation, Plant, Plant Tumors, Meloidogyne incognita, Arabidopsis thaliana, Cytoskeleton, Research Articles, filament turnover, 0303 health sciences, EPS-1, biology, giant-cells, cytoskeleton, cell periphery, maize actin, Cell biology, Actin Depolymerizing Factors, RNA, Plant, Gene Knockdown Techniques, RNA Interference, macromolecular substances, [SDV.GEN.GPL]Life Sciences [q-bio]/Genetics/Plants genetics, 03 medical and health sciences, Multinucleate, medicine, Animals, Root-knot nematode, nonhost resistance, Tylenchoidea, RELATION HOTE-PARASITE, 030304 developmental biology, Arabidopsis Proteins, plant-parasitic nematodes, Laboratorium voor Celbiologie, Cell Biology, adf/cofilin family, medicine.disease, biology.organism_classification, gene-expression, Actins, Laboratory of Cell Biology, Nematode infection, Giant cell, 010606 plant biology & botany
Abstract: Reorganization of the actin and microtubule networks is known to occur in targeted vascular parenchymal root cells upon infection with the nematode Meloidogyne incognita. Here, we show that actin-depolymerizing factor (ADF) is upregulated in the giant feeding cells of Arabidopsis thaliana that develop upon nematode infection and that knockdown of a specific ADF isotype inhibits nematode proliferation. Analysis of the levels of transcript and the localization of seven ADF genes shows that five are upregulated in galls that result from the infection and that ADF2 expression is particularly increased between 14 and 21 d after nematode inoculation. Further analysis of ADF2 function in inducible RNA interference lines designed to knock down ADF2 expression reveals that this protein is required for normal cell growth and plant development. The net effect of decreased levels of ADF2 is F-actin stabilization in cells, resulting from decreased F-actin turnover. In nematode-infected plants with reduced levels of ADF2, the galls containing the giant feeding cells and growing nematodes do not develop due to the arrest in growth of the giant multinucleate feeding cells, which in turn is due to an aberrant actin network.
Published: 2009

37. Interaction of pollen-specific actin-depolymerizing factor with actin

Author: Sutherland K. Maciver, Ellen G. Allwood, Andrei Smertenko, Alan G. Weeds, Patrick J. Hussey, Chang-Jie Jiang, and Safina Khan
Subjects: Actin depolymerizing factor, Pollen, Genetics, Pollen specific, medicine, Cell Biology, Plant Science, Biology, medicine.disease_cause, Actin, Cell biology
Published: 2008

38. A novel role for the nuclear membrane protein emerin in association of the centrosome to the outer nuclear membrane

Author: Patrick J. Hussey, Irena Hausmanowa-Petrucewicz, Christopher J. Hutchison, Georgia Salpingidou, and Andrei Smertenko
Subjects: Cell Nucleus, Centrosome, Nuclear Envelope, LINC complex, Emerin, Membrane Proteins, Nuclear Proteins, Cell Biology, Biology, Fibroblasts, Actin cytoskeleton, Cell biology, Tubulin, Report, Nuclear lamina, Inner membrane, Humans, Nuclear protein, Cytoskeleton, Research Articles, Cells, Cultured, Protein Binding
Abstract: The type II inner nuclear membrane protein emerin is a component of the LINC complex that connects the nuclear lamina to the actin cytoskeleton. In emerin-null or -deficient human dermal fibroblasts we find that the centrosome is detached from the nucleus. Moreover, following siRNA knockdown of emerin in wild-type fibroblasts, the centrosome also becomes detached from the nucleus. We show that emerin interacts with tubulin, and that nocadozole-treated wild-type cells phenocopy the detached centrosome characteristic of emerin-null/deficient cells. We also find that a significant fraction of emerin is located at the outer nuclear membrane and peripheral ER, where it interacts directly with the centrosome. Our data provide the first evidence in mammalian cells as to the nature of the linkage of the centrosome, and therefore the tubulin cytoskeleton, with the outer nuclear membrane.
Published: 2007

39. Control of the AtMAP65-1 interaction with microtubules through the cell cycle

Author: Patrick J. Hussey, Laci Bögre, Stepan Fenyk, Hsin-Yu Chang, Andrei Smertenko, Seiji Sonobe, and Magdalena Weingartner
Subjects: Recombinant Fusion Proteins, Arabidopsis, Spindle Apparatus, Aster (cell biology), Biology, Microtubules, Tobacco, Cleavage furrow, Phosphorylation, Prometaphase, Metaphase, Cells, Cultured, Microtubule nucleation, Anaphase, Arabidopsis Proteins, Cell Cycle, Spindle midzone, Cell Biology, Cyclin-Dependent Kinases, Peptide Fragments, Cell biology, Mitogen-Activated Protein Kinases, Astral microtubules, Microtubule-Associated Proteins, Fluorescence Recovery After Photobleaching, Signal Transduction
Abstract: Cell division depends on the fine control of both microtubule dynamics and microtubule organisation. The microtubule bundling protein MAP65 is a `midzone MAP' essential for the integrity of the anaphase spindle and cell division. Arabidopsis thaliana MAP65-1 (AtMAP65-1) binds and bundles microtubules by forming 25 nm cross-bridges. Moreover, as AtMAP65-1 bundles microtubules in interphase, anaphase and telophase but does not bind microtubules in prophase or metaphase, its activity through the cell cycle must be under tight control. Here we show that AtMAP65-1 is hyperphosphorylated during prometaphase and metaphase and that CDK and MAPK are involved in this phosphorylation. This phosphorylation inhibits AtMAP65-1 activity. Expression of non-phosphorylatable AtMAP65-1 has a negative effect on mitotic progression resulting in excessive accumulation of microtubules in the metaphase spindle midzone causing a delay in mitosis. We conclude that normal metaphase spindle organisation and the transition to anaphase is dependent on inactivation of AtMAP65-1.
Published: 2006

40. Cysteine protease mcII-Pa executes programmed cell death during plant embryogenesis

Author: Lada Filonova, Andrey A. Zamyatnin, Boris Zhivotovsky, Maria F. Suarez, Salvador Rodriguez-Nieto, Peter V. Bozhkov, Geoffrey Daniel, and Andrei Smertenko
Subjects: Programmed cell death, Proteases, Immunoblotting, Molecular Sequence Data, Plant embryogenesis, Apoptosis, DNA Fragmentation, Substrate Specificity, In Situ Nick-End Labeling, otorhinolaryngologic diseases, Picea, Caspase, Cell Nucleus, Multidisciplinary, Base Sequence, biology, Sequence Analysis, DNA, Biological Sciences, Immunohistochemistry, Cysteine protease, Metacaspase, Chromatin, Cell biology, Cysteine Endopeptidases, Kinetics, Microscopy, Electron, Microscopy, Fluorescence, Biochemistry, biology.protein
Abstract: Programmed cell death (PCD) is indispensable for eukaryotic development. In animals, PCD is executed by the caspase family of cysteine proteases. Plants do not have close homologues of caspases but possess a phylogenetically distant family of cysteine proteases named metacaspases. The cellular function of metacaspases in PCD is unknown. Here we show that during plant embryogenesis, metacaspase mcII-Pa translocates from the cytoplasm to nuclei in terminally differentiated cells that are destined for elimination, where it colocalizes with the nuclear pore complex and chromatin, causing nuclear envelope disassembly and DNA fragmentation. The cell-death function of mcII-Pa relies on its cysteine-dependent arginine-specific proteolytic activity. Accordingly, mutation of catalytic cysteine abrogates the proteolytic activity of mcII-Pa and blocks nuclear degradation. These results establish metacaspase as an executioner of PCD during embryo patterning and provide a functional link between PCD and embryogenesis in plants. Although mcII-Pa and metazoan caspases have different substrate specificity, they serve a common function during development, demonstrating the evolutionary parallelism of PCD pathways in plants and animals.
Published: 2005

41. Dynamic interaction of NtMAP65-1a with microtubules in vivo

Author: David P. Dixon, Patrick J. Hussey, Andrei Smertenko, Hsin-Yu Chang, and Hisako Igarashi
Subjects: Arabidopsis Proteins, Microtubule-associated protein, Spindle midzone, Arabidopsis, Mitosis, Cell Biology, Surface Plasmon Resonance, Biology, Aster (cell biology), Microtubules, Cell biology, Treadmilling, Tubulin, Tobacco, biology.protein, Basal body, Astral microtubules, Dimerization, Microtubule-Associated Proteins, Fluorescence Recovery After Photobleaching, Plant Proteins, Microtubule nucleation
Abstract: Plant microtubules are intrinsically more dynamic than those from animals. We know little about the dynamics of the interaction of plant microtubule-associated proteins (MAPs) with microtubules. Here, we have used tobacco and Arabidopsis MAPs with relative molecular mass 65 kDa (NtMAP65-1a and AtMAP65-1), to study their interaction with microtubules in vivo. Using fluorescence recovery after photobleaching we report that the turnover of both NtMAP65-1a and AtMAP65-1 bound to microtubules is four- to fivefold faster than microtubule treadmilling (13 seconds compared with 56 seconds, respectively) and that the replacement of NtMAP65-1a on microtubules is by random association rather than by translocation along microtubules. MAP65 will only bind polymerised microtubules and not its component tubulin dimers. The turnover of NtMAP65-1a and AtMAP65-1 on microtubules is similar in the interphase cortical array, the preprophase band and the phragmoplast, strongly suggesting that their role in these arrays is the same. NtMAP65-1a and AtMAP65-1 are not observed to bind microtubules in the metaphase spindle and their rate of recovery is consistent with their cytoplasmic localisation. In addition, the dramatic reappearance of NtMAP65-1a on microtubules at the spindle midzone in anaphase B suggests that NtMAP65-1a is controlled post-translationally. We conclude that the dynamic properties of these MAPs in vivo taken together with the fact that they have been shown not to effect microtubule polymerisation in vitro, makes them ideally suited to a role in crossbridging microtubules that need to retain spatial organisation in rapidly reorganising microtubule arrays.
Published: 2005

42. Direct observation of UV-B radiation effect on antigen–antibody coupling using surface plasmon resonance

Author: E.R. Surovtseva, Yu.M. Shirshov, P.S. Smertenko, and A.S. Majstrenko
Subjects: biology, Chemistry, Kinetics, Metals and Alloys, Analytical chemistry, Tryptophan, Quantum yield, Condensed Matter Physics, Photochemistry, Surfaces, Coatings and Films, Electronic, Optical and Magnetic Materials, Coupling (electronics), Materials Chemistry, biology.protein, Irradiation, Electrical and Electronic Engineering, Surface plasmon resonance, Bovine serum albumin, Tyrosine, Instrumentation
Abstract: We studied the effect of UV irradiation on (non)specific bounding of bovine serum albumin (BSA) and mouse antiBSA immunoglobulin (IgG) using a surface plasmon resonance (SPR) apparatus Biosuplar-2 and special photodetectors. It was found that specific bounding of AG–AB complex is broken under UV irradiation. Contrary to this, UV irradiation of BSA layer before its contact with IgG did not demonstrate any peculiarities. On the basis of quantitative determination of kinetics of specific bounding and washing and precise measurement of photon flux, the product γσ of quantum yield γ and active centre cross-section σ was evaluated to be about 10 −20 cm 2 . As the dimension of amino acid residues tryptophan and tyrosine is about 1 nm, we have concluded that the quantum yield of reaction is very small (about 0.001). This indicates at presence of a barrier for direct photochemical reaction between the interacting substances.
Published: 2005

43. VEIDase is a principal caspase-like activity involved in plant programmed cell death and essential for embryonic pattern formation

Author: Andrei Smertenko, Boris Zhivotovsky, Maria F. Suarez, Peter V. Bozhkov, S. von Arnold, Andreas Helmersson, and Lada Filonova
Subjects: Cell Extracts, Programmed cell death, biology, Somatic embryogenesis, Temperature, Plant embryogenesis, Apoptosis, Embryo, Cell Biology, Hydrogen-Ion Concentration, Sodium Chloride, Caspase Inhibitors, Embryonic stem cell, Metacaspase, Cell biology, Zinc, Caspases, Seeds, biology.protein, Protease Inhibitors, Picea, Molecular Biology, Caspase, Body Patterning
Abstract: Plant embryogenesis is intimately associated with programmed cell death. The mechanisms of initiation and control of programmed cell death during plant embryo development are not known. Proteolytic activity associated with caspase-like proteins is paramount for control of programmed cell death in animals and yeasts. Caspase family of proteases has unique strong preference for cleavage of the target proteins next to asparagine residue. In this work, we have used synthetic peptide substrates containing caspase recognition sites and corresponding specific inhibitors to analyse the role of caspase-like activity in the regulation of programmed cell death during plant embryogenesis. We demonstrate that VEIDase is a principal caspase-like activity implicated in plant embryogenesis. This activity increases at the early stages of embryo development that coincide with massive cell death during shape remodeling. The VEIDase activity exhibits high sensitivity to pH, ionic strength and Zn(2+) concentration. Altogether, biochemical assays show that VEIDase plant caspase-like activity resembles that of both mammalian caspase-6 and yeast metacaspase, YCA1. In vivo, VEIDase activity is localised specifically in the embryonic cells during both the commitment and in the beginning of the execution phase of programmed cell death. Inhibition of VEIDase prevents normal embryo development via blocking the embryo-suspensor differentiation. Our data indicate that the VEIDase activity is an integral part in the control of plant developmental cell death programme, and that this activity is essential for the embryo pattern formation.
Published: 2003

44. Regulation of the Pollen-Specific Actin-Depolymerizing Factor LlADF1

Author: Richard G. Anthony, John H. Doonan, Alan G. Weeds, Patrick J. Hussey, Andrei Smertenko, Ellen G. Allwood, Bjørn K. Drøbak, and Stefanie Reichelt
Subjects: Arabidopsis, Arp2/3 complex, Saccharomyces cerevisiae, macromolecular substances, Plant Science, medicine.disease_cause, Zea mays, Magnoliopsida, Gene Expression Regulation, Plant, Two-Hybrid System Techniques, Pollen, otorhinolaryngologic diseases, medicine, Cloning, Molecular, Phosphorylation, Conserved Sequence, Cytoskeleton, Phospholipids, Phylogeny, Actin, Plant Proteins, biology, Arabidopsis Proteins, Brassica napus, Microfilament Proteins, food and beverages, Actin remodeling, Cell Biology, Hydrogen-Ion Concentration, Actin cytoskeleton, Actins, Cell biology, Destrin, Actin Depolymerizing Factors, Profilin, Actin depolymerizing factor, biology.protein, Pollen tube, Lilium, Carrier Proteins, Research Article
Abstract: Pollen tube growth is dependent on a dynamic actin cytoskeleton, suggesting that actin-regulating proteins are involved. We have examined the regulation of the lily pollen-specific actin-depolymerizing factor (ADF) LlADF1. Its actin binding and depolymerizing activity is pH sensitive, inhibited by certain phosphoinositides, but not controlled by phosphorylation. Compared with its F-actin binding properties, its low activity in depolymerization assays has been used to explain why pollen ADF decorates F-actin in pollen grains. This low activity is incompatible with a role in increasing actin dynamics necessary to promote pollen tube growth. We have identified a plant homolog of actin-interacting protein, AIP1, which enhances the depolymerization of F-actin in the presence of LlADF1 by approximately 60%. Both pollen ADF and pollen AIP1 bind F-actin in pollen grains but are mainly cytoplasmic in pollen tubes. Our results suggest that together these proteins remodel actin filaments as pollen grains enter and exit dormancy.
Published: 2002

45. MOR1/GEM1 has an essential role in the plant-specific cytokinetic phragmoplast

Author: Timothy J. Hawkins, Renate Schmidt, Daniel Schubert, David Twell, Soon Ki Park, Andrei Smertenko, and Patrick J. Hussey
Subjects: DNA, Plant, Swine, Microtubule-associated protein, Molecular Sequence Data, Mutant, Arabidopsis, In Vitro Techniques, Biology, Genes, Plant, Phragmoplast, Microtubules, Article, Microtubule, Animals, Amino Acid Sequence, Cytoskeleton, Plant Proteins, Base Sequence, Arabidopsis Proteins, Genetic Complementation Test, Brain, Cell Biology, Chromatin, Cell biology, Phenotype, Mutation, Astral microtubules, Microtubule-Associated Proteins, Cell Division, Cytokinesis
Abstract: MOR1 is a member of the MAP215 family of microtubule-associated proteins and is required to establish interphase arrays of cortical microtubules in plant cells1. Here we show that MOR1 binds microtubules in vivo, localizing to both cortical microtubules and to areas of overlapping microtubules in the phragmoplast. Genetic complementation of the cytokinesis-defective gemini pollen 1-1 (gem1-1) mutation with MOR1 shows that MOR1 (which is synonymous with the protein GEM1) is essential in cytokinesis. Phenotypic analysis of gem1-1 and gem1-2, which contains a T-DNA insertion, confirm that MOR1/GEM1 is essential for regular patterns of cytokinesis. Both the gem1-1 and gem1-2 mutations cause the truncation of the MOR1/GEM1 protein. In addition, the carboxy-terminal domain of the protein, which is absent in both mutants, binds microtubules in vitro. Our data show that MOR1/GEM1 has an essential role in the cytokinetic phragmoplast.
Published: 2002

46. [Untitled]

Author: Despina Kaloriti, Patrick J. Hussey, Hisako Igarashi, Andrei Smertenko, and Timothy J. Hawkins
Subjects: Tobacco BY-2 cells, Cell division, Microtubule-associated protein, Microtubule organizing center, Plant Science, General Medicine, Biology, Cell biology, Tubulin, Microtubule, Genetics, biology.protein, Cytoskeleton, Agronomy and Crop Science, Microtubule nucleation
Abstract: The microtubule cytoskeleton is a dynamic filamentous structure involved in many key processes in plant cell morphogenesis including nuclear and cell division, deposition of cell wall, cell expansion, organelle movement and secretion. The principal microtubule protein is tubulin, which associates to form the wall of the tubule. In addition, various associated proteins bind microtubules either to anchor, cross-link or regulate the microtubule network within cells. Biochemical, molecular biological and genetic approaches are being successfully used to identify these microtubule-associated proteins (MAPs) in plants, and we describe recent progress on three of these proteins.
Published: 2002

47. Somatic embryogenesis: life and death processes during apical-basal patterning

Author: Peter V. Bozhkov and Andrei Smertenko
Subjects: Plant Somatic Embryogenesis Techniques, Programmed cell death, Zygote, Somatic embryogenesis, Physiology, Embryogenesis, Plant Development, Embryo, Apoptosis, Plant Science, Biology, Cell fate determination, Plants, Cell biology, Homologous chromosome, Suspensor, Plant Physiological Phenomena, Cell Proliferation, Plant Proteins
Abstract: Somatic embryogenesis (SE) is a process of differentiation of cells into a plant bypassing the fusion of gametes. As such, it represents a very powerful tool in biotechnology for propagation of species with a long reproductive cycle or low seed set and production of genetically modified plants with improved traits. SE is also a versatile model to study cellular and molecular mechanisms of plant embryo patterning. The morphology and molecular regulation of SE resemble those of zygotic embryogenesis and begin with establishment of apical-basal asymmetry. The apical domain, the embryo proper, proliferates and eventually gives rise to the plantlet, while the basal part, the embryo suspensor, is terminally differentiated and gradually removed via vacuolar programmed cell death (PCD). This PCD is essential for normal development of the apical domain. Emerging evidence demonstrates that signalling events in the apical and basal domains share homologous components. Here we provide an overview of the main pathways controlling the life and death events during SE.
Published: 2014

48. Phosphorylation of plant actin-depolymerising factor by calmodulin-like domain protein kinase

Author: Ellen G. Allwood, Andrei Smertenko, and Patrick J. Hussey
Subjects: Calmodulin, Blotting, Western, Protein domain, Higher plant, Biophysics, macromolecular substances, Biology, Zea mays, environment and public health, Biochemistry, Calmodulin-like domain protein kinase, MAP2K7, Phosphoserine, Structural Biology, Genetics, Animals, Protein phosphorylation, Enzyme Inhibitors, Phosphorylation, Muscle, Skeletal, Protein Kinase Inhibitors, Molecular Biology, Cytoskeleton, Plant Proteins, Plants, Medicinal, Kinase, Microfilament Proteins, Cyclin-dependent kinase 2, Fabaceae, Cell Biology, Cofilin, Cell biology, Destrin, Actin Depolymerizing Factors, biology.protein, Actin-depolymerizing factor, Rabbits, Protein Kinases
Abstract: The actin-depolymerising factor (ADF)/cofilin group of proteins are stimulus-responsive actin-severing proteins, members of which are regulated by reversible phosphorylation. The phosphorylation site on the maize ADF, ZmADF3, is Ser-6 but the kinase responsible is unknown [Smertenko et al., Plant J. 14 (1998) 187–193]. We have partially purified the ADF kinase(s) and found it to be calcium-regulated and inhibited by N-(6-aminohexyl)-[3H]5-chloro-1-naphthalenesulphonamide. Immunoblotting reveals that calmodulin-like domain protein kinase(s) (CDPK) are enriched in the purified preparation and addition of anti-CDPK to in vitro phosphorylation assays results in the inhibition of ADF phosphorylation. These data strongly suggest that plant ADF is phosphorylated by CDPK(s), a class of protein kinases unique to plants and protozoa.
Published: 2001

49. TOXIN EVOLUTION IN SCORPION VENOM: EVIDENCE FOR TOXIN DIVERGENCE UNDER STRONG NEGATIVE SELECTION INLEIURUS QUINQUESTRIATUSSUBSPECIES

Author: Patrick J. Hussey, Andrei Smertenko, Mohamed Alaa A. Omran, and Alistair McVean
Subjects: biology, Leiurus, Health, Toxicology and Mutagenesis, Scorpion, Zoology, Venom, Subspecies, Toxicology, biology.organism_classification, Divergence, Negative selection, Molecular evolution, Buthidae, biology.animal
Abstract: The Buthid scorpion Leiurus quinquestriatus is divided into two sub-species whose region of contact occurs at the Suez Isthmus. L.q. quinquestriatus, found in the North Africa is distinguished from L.q. hebraeus by minor differences in morphology. Despite the very high similarity in body plan, out of the 24 toxins isolated from this species none is common to both sub-species, suggesting a degree of molecular divergence not apparent at the morphological level. We show, by comparison with two sets of reference proteins from humans and Old-World monkeys, that divergence of toxins with common structures and functions in these two sub-species has occurred under conditions of strong negative selection. Potential selection pressures responsible for toxin divergence are discussed, including the role of conflicting interests during courtship.
Published: 2001

50. The Life and Death Signalling Underlying Cell Fate Determination During Somatic Embryogenesis

Author: Peter V. Bozhkov and Andrei Smertenko
Subjects: Programmed cell death, Somatic embryogenesis, Cytoplasm, Embryogenesis, Botany, Embryo, Biology, Cell fate determination, Meristem, Suspensor, Cell biology
Abstract: Somatic embryogenesis (SE) is a sequence of stereotypical morphological transformations, which results in differentiation of cells into a plant body bypassing the fusion of gametes. As such, it represents a very powerful tool in biotechnology to propagate species with long reproductive cycles or low seed set and the production of genetically modified plants with improved traits. The initiation of SE can be divided into five major stages: (i) perception of extracellular signals or stress stimuli, (ii) transduction of the extracellular signal through the cytoplasm into the nucleus, (iii) induction of gene transcription required for embryogenesis, (iv) reorganisation of cytoplasm and (v) onset of embryonic development. The further embryonic development during SE resembles its zygotic counterpart and begins with the establishment of apical-basal asymmetry. The apical domain, the embryo proper, proliferates and eventually gives rise to the plantlet, while the basal part, the embryo suspensor, becomes a subject of terminal differentiation and gradually degrades via vacuolar programmed cell death (PCD). This PCD is essential for normal development of the apical domain. Some signalling events in the apical and basal domains share homologous components. Here, we describe our current knowledge on the control of life and death processes during SE.
Published: 2013

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