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1. A pseudoautosomal glycosylation disorder prompts the revision of dolichol biosynthesis

Author: Wilson, Matthew P., Kentache, Takfarinas, Althoff, Charlotte R., Schulz, Céline, de Bettignies, Geoffroy, Mateu Cabrera, Gisèle, Cimbalistiene, Loreta, Burnyte, Birute, Yoon, Grace, Costain, Gregory, Vuillaumier-Barrot, Sandrine, Cheillan, David, Rymen, Daisy, Rychtarova, Lucie, Hansikova, Hana, Bury, Marina, Dewulf, Joseph P., Caligiore, Francesco, Jaeken, Jaak, Cantagrel, Vincent, Van Schaftingen, Emile, Matthijs, Gert, Foulquier, François, and Bommer, Guido T.
Published: 2024
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2. A non-coding variant in the Kozak sequence of RARS2 strongly decreases protein levels and causes pontocerebellar hypoplasia

Author: Nicolle, Romain, Altin, Nami, Siquier-Pernet, Karine, Salignac, Sherlina, Blanc, Pierre, Munnich, Arnold, Bole-Feysot, Christine, Malan, Valérie, Caron, Barthélémy, Nitschké, Patrick, Desguerre, Isabelle, Boddaert, Nathalie, Rio, Marlène, Rausell, Antonio, and Cantagrel, Vincent
Published: 2023
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3. De novo variants in DENND5B cause a neurodevelopmental disorder

Author: Acosta, Maria T., Adams, David R., Alvarez, Raquel L., Alvey, Justin, Allworth, Aimee, Andrews, Ashley, Ashley, Euan A., Afzali, Ben, Bacino, Carlos A., Bademci, Guney, Balasubramanyam, Ashok, Baldridge, Dustin, Bale, Jim, Bamshad, Michael, Barbouth, Deborah, Bayrak-Toydemir, Pinar, Beck, Anita, Beggs, Alan H., Behrens, Edward, Bejerano, Gill, Bellen, Hugo J., Bennett, Jimmy, Bernstein, Jonathan A., Berry, Gerard T., Bican, Anna, Bivona, Stephanie, Blue, Elizabeth, Bohnsack, John, Bonner, Devon, Botto, Lorenzo, Briere, Lauren C., Brown, Gabrielle, Burke, Elizabeth A., Burrage, Lindsay C., Butte, Manish J., Byers, Peter, Byrd, William E., Carey, John, Carrasquillo, Olveen, Cassini, Thomas, Chang, Ta Chen Peter, Chanprasert, Sirisak, Chao, HsiaoTuan, Chinn, Ivan, Clark, Gary D., Coakley, Terra R., Cobban, Laurel A., Cogan, Joy D., Coggins, Matthew, Cole, F. Sessions, Colley, Heather A., Cope, Heidi, Corona, Rosario, Craigen, William J., Crouse, Andrew B., Cunningham, Michael, D’Souza, Precilla, Dai, Hongzheng, Dasari, Surendra, Davis, Joie, Dayal, Jyoti G., Delgado, Margaret, Dell'Angelica, Esteban C., Dipple, Katrina, Doherty, Daniel, Dorrani, Naghmeh, Doss, Argenia L., Douine, Emilie D., Earl, Dawn, Eckstein, David J., Emrick, Lisa T., Eng, Christine M., Falk, Marni, Fieg, Elizabeth L., Fisher, Paul G., Fogel, Brent L., Forghani, Irman, Fu, Jiayu, Gahl, William A., Glass, Ian, Goddard, Page C., Godfrey, Rena A., Grajewski, Alana, Gropman, Andrea, Halley, Meghan C., Hamid, Rizwan, Hanchard, Neal, Hassey, Kelly, Hayes, Nichole, High, Frances, Hing, Anne, Hisama, Fuki M., Holm, Ingrid A., Hom, Jason, Horike-Pyne, Martha, Huang, Alden, Huang, Yan, Hutchison, Sarah, Introne, Wendy, Isasi, Rosario, Izumi, Kosuke, Jarvik, Gail P., Jarvik, Jeffrey, Jayadev, Suman, Jean-Marie, Orpa, Jobanputra, Vaidehi, Kaitryn, Emerald, Ketkar, Shamika, Kiley, Dana, Kilich, Gonench, Kobren, Shilpa N., Kohane, Isaac S., Kohler, Jennefer N., Korrick, Susan, Krakow, Deborah, Krasnewich, Donna M., Kravets, Elijah, Lalani, Seema R., Lam, Byron, Lam, Christina, Lanpher, Brendan C., Lanza, Ian R., LeBlanc, Kimberly, Lee, Brendan H., Levitt, Roy, Lewis, Richard A., Liu, Pengfei, Liu, Xue Zhong, Longo, Nicola, Loo, Sandra K., Loscalzo, Joseph, Maas, Richard L., Macnamara, Ellen F., MacRae, Calum A., Maduro, Valerie V., Maghiro, AudreyStephannie, Mahoney, Rachel, Malicdan, May Christine V., Mamounas, Laura A., Manolio, Teri A., Mao, Rong, Marom, Ronit, Marth, Gabor, Martin, Beth A., Martin, Martin G., Martínez-Agosto, Julian A., Marwaha, Shruti, McCauley, Jacob, McConkie-Rosell, Allyn, McCray, Alexa T., McGee, Elisabeth, Might, Matthew, Miller, Danny, Mirzaa, Ghayda, Morava, Eva, Moretti, Paolo, Morimoto, Marie, Mulvihill, John J., Nakano-Okuno, Mariko, Nelson, Stanley F., Nieves-Rodriguez, Shirley, Novacic, Donna, Oglesbee, Devin, Orengo, James P., Pace, Laura, Pak, Stephen, Pallais, J. Carl, Papp, Jeanette C., Parker, Neil H., Petcharet, Leoyklang, Phillips, John A., III, Posey, Jennifer E., Potocki, Lorraine, Swerdzewski, Barbara N. Pusey, Quinlan, Aaron, Rao, Deepak A., Raper, Anna, Raskind, Wendy, Renteria, Genecee, Reuter, Chloe M., Rives, Lynette, Robertson, Amy K., Rodan, Lance H., Rosenfeld, Jill A., Rosenthal, Elizabeth, Rossignol, Francis, Ruzhnikov, Maura, Sabaii, Marla, Sacco, Ralph, Sampson, Jacinda B., Saporta, Mario, Schaechter, Judy, Schedl, Timothy, Schoch, Kelly, Scott, Daryl A., Seto, Elaine, Sharma, Prashant, Shashi, Vandana, Shelkowitz, Emily, Sheppeard, Sam, Shin, Jimann, Silverman, Edwin K., Sinsheimer, Janet S., Sisco, Kathy, Smith, Edward C., Smith, Kevin S., Solnica-Krezel, Lilianna, Solomon, Ben, Spillmann, Rebecca C., Stergachis, Andrew, Stoler, Joan M., Sullivan, Kathleen, Sullivan, Jennifer A., Sutton, Shirley, Sweetser, David A., Sybert, Virginia, Tabor, Holly K., Tan, Queenie K.-G., Tan, Amelia L.M., Tarakad, Arjun, Taylor, Herman, Tekin, Mustafa, Telischi, Fred, Thorson, Willa, Tifft, Cynthia J., Toro, Camilo, Tran, Alyssa A., Ungar, Rachel A., Urv, Tiina K., Vanderver, Adeline, Velinder, Matt, Viskochil, Dave, Vogel, Tiphanie P., Wahl, Colleen E., Walker, Melissa, Walley, Nicole M., Wambach, Jennifer, Wan, Jijun, Wang, Lee-kai, Wangler, Michael F., Ward, Patricia A., Wegner, Daniel, Weisz Hubshman, Monika, Wener, Mark, Wenger, Tara, Westerfield, Monte, Wheeler, Matthew T., Whitlock, Jordan, Wolfe, Lynne A., Worley, Kim, Yamamoto, Shinya, Zhang, Zhe, Zuchner, Stephan, Scala, Marcello, Tomati, Valeria, Ferla, Matteo, Lena, Mariateresa, Cohen, Julie S., Fatemi, Ali, Brokamp, Elly, Koziura, Mary E., Nicouleau, Michael, Rio, Marlene, Siquier, Karine, Boddaert, Nathalie, Musante, Ilaria, Tamburro, Serena, Baldassari, Simona, Iacomino, Michele, Scudieri, Paolo, Bellus, Gary, Reed, Sara, Al Saif, Hind, Russo, Rossana Sanchez, Walsh, Matthew B., Cantagrel, Vincent, Crunk, Amy, Gustincich, Stefano, Ruggiero, Sarah M., Fitzgerald, Mark P., Helbig, Ingo, Striano, Pasquale, Severino, Mariasavina, Salpietro, Vincenzo, Pedemonte, Nicoletta, and Zara, Federico
Published: 2024
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4. 16p13.11p11.2 triplication syndrome: a new recognizable genomic disorder characterized by optical genome mapping and whole genome sequencing

Author: Nicolle, Romain, Siquier-Pernet, Karine, Rio, Marlène, Guimier, Anne, Ollivier, Emmanuelle, Nitschke, Patrick, Bole-Feysot, Christine, Romana, Serge, Hastie, Alex, Cantagrel, Vincent, and Malan, Valérie
Published: 2022
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5. Genotype–phenotype correlations in individuals with pathogenic RERE variants

Author: Jordan, Valerie K, Fregeau, Brieana, Ge, Xiaoyan, Giordano, Jessica, Wapner, Ronald J, Balci, Tugce B, Carter, Melissa T, Bernat, John A, Moccia, Amanda N, Srivastava, Anshika, Martin, Donna M, Bielas, Stephanie L, Pappas, John, Svoboda, Melissa D, Rio, Marlène, Boddaert, Nathalie, Cantagrel, Vincent, Lewis, Andrea M, Scaglia, Fernando, Network, Undiagnosed Diseases, Kohler, Jennefer N, Bernstein, Jonathan A, Dries, Annika M, Rosenfeld, Jill A, DeFilippo, Colette, Thorson, Willa, Yang, Yaping, Sherr, Elliott H, Bi, Weimin, and Scott, Daryl A
Subjects: Congenital Structural Anomalies, Genetics, Genetic Testing, Rare Diseases, Pediatric, Aetiology, 2.1 Biological and endogenous factors, Adolescent, Carrier Proteins, Child, Preschool, Fatal Outcome, Female, Genetic Association Studies, Humans, Infant, Male, Mutation, Young Adult, 1p36 deletion syndrome, CHARGE syndrome, CHD7, genotype-phenotype correlations, NEDBEH, RERE, Undiagnosed Diseases Network, Clinical Sciences, Genetics & Heredity
Abstract: Heterozygous variants in the arginine-glutamic acid dipeptide repeats gene (RERE) have been shown to cause neurodevelopmental disorder with or without anomalies of the brain, eye, or heart (NEDBEH). Here, we report nine individuals with NEDBEH who carry partial deletions or deleterious sequence variants in RERE. These variants were found to be de novo in all cases in which parental samples were available. An analysis of data from individuals with NEDBEH suggests that point mutations affecting the Atrophin-1 domain of RERE are associated with an increased risk of structural eye defects, congenital heart defects, renal anomalies, and sensorineural hearing loss when compared with loss-of-function variants that are likely to lead to haploinsufficiency. A high percentage of RERE pathogenic variants affect a histidine-rich region in the Atrophin-1 domain. We have also identified a recurrent two-amino-acid duplication in this region that is associated with the development of a CHARGE syndrome-like phenotype. We conclude that mutations affecting RERE result in a spectrum of clinical phenotypes. Genotype-phenotype correlations exist and can be used to guide medical decision making. Consideration should also be given to screening for RERE variants in individuals who fulfill diagnostic criteria for CHARGE syndrome but do not carry pathogenic variants in CHD7.
Published: 2018

6. De novo variants in DENND5B cause a neurodevelopmental disorder

Author: Scala, Marcello, primary, Tomati, Valeria, additional, Ferla, Matteo, additional, Lena, Mariateresa, additional, Cohen, Julie S., additional, Fatemi, Ali, additional, Brokamp, Elly, additional, Bican, Anna, additional, Phillips, John A., additional, Koziura, Mary E., additional, Nicouleau, Michael, additional, Rio, Marlene, additional, Siquier, Karine, additional, Boddaert, Nathalie, additional, Musante, Ilaria, additional, Tamburro, Serena, additional, Baldassari, Simona, additional, Iacomino, Michele, additional, Scudieri, Paolo, additional, Rosenfeld, Jill A., additional, Bellus, Gary, additional, Reed, Sara, additional, Al Saif, Hind, additional, Russo, Rossana Sanchez, additional, Walsh, Matthew B., additional, Cantagrel, Vincent, additional, Crunk, Amy, additional, Gustincich, Stefano, additional, Ruggiero, Sarah M., additional, Fitzgerald, Mark P., additional, Helbig, Ingo, additional, Striano, Pasquale, additional, Severino, Mariasavina, additional, Salpietro, Vincenzo, additional, Pedemonte, Nicoletta, additional, Zara, Federico, additional, Acosta, Maria T., additional, Adams, David R., additional, Alvarez, Raquel L., additional, Alvey, Justin, additional, Allworth, Aimee, additional, Andrews, Ashley, additional, Ashley, Euan A., additional, Afzali, Ben, additional, Bacino, Carlos A., additional, Bademci, Guney, additional, Balasubramanyam, Ashok, additional, Baldridge, Dustin, additional, Bale, Jim, additional, Bamshad, Michael, additional, Barbouth, Deborah, additional, Bayrak-Toydemir, Pinar, additional, Beck, Anita, additional, Beggs, Alan H., additional, Behrens, Edward, additional, Bejerano, Gill, additional, Bellen, Hugo J., additional, Bennett, Jimmy, additional, Bernstein, Jonathan A., additional, Berry, Gerard T., additional, Bivona, Stephanie, additional, Blue, Elizabeth, additional, Bohnsack, John, additional, Bonner, Devon, additional, Botto, Lorenzo, additional, Briere, Lauren C., additional, Brown, Gabrielle, additional, Burke, Elizabeth A., additional, Burrage, Lindsay C., additional, Butte, Manish J., additional, Byers, Peter, additional, Byrd, William E., additional, Carey, John, additional, Carrasquillo, Olveen, additional, Cassini, Thomas, additional, Chang, Ta Chen Peter, additional, Chanprasert, Sirisak, additional, Chao, HsiaoTuan, additional, Chinn, Ivan, additional, Clark, Gary D., additional, Coakley, Terra R., additional, Cobban, Laurel A., additional, Cogan, Joy D., additional, Coggins, Matthew, additional, Cole, F. Sessions, additional, Colley, Heather A., additional, Cope, Heidi, additional, Corona, Rosario, additional, Craigen, William J., additional, Crouse, Andrew B., additional, Cunningham, Michael, additional, D’Souza, Precilla, additional, Dai, Hongzheng, additional, Dasari, Surendra, additional, Davis, Joie, additional, Dayal, Jyoti G., additional, Delgado, Margaret, additional, Dell'Angelica, Esteban C., additional, Dipple, Katrina, additional, Doherty, Daniel, additional, Dorrani, Naghmeh, additional, Doss, Argenia L., additional, Douine, Emilie D., additional, Earl, Dawn, additional, Eckstein, David J., additional, Emrick, Lisa T., additional, Eng, Christine M., additional, Falk, Marni, additional, Fieg, Elizabeth L., additional, Fisher, Paul G., additional, Fogel, Brent L., additional, Forghani, Irman, additional, Fu, Jiayu, additional, Gahl, William A., additional, Glass, Ian, additional, Goddard, Page C., additional, Godfrey, Rena A., additional, Grajewski, Alana, additional, Gropman, Andrea, additional, Halley, Meghan C., additional, Hamid, Rizwan, additional, Hanchard, Neal, additional, Hassey, Kelly, additional, Hayes, Nichole, additional, High, Frances, additional, Hing, Anne, additional, Hisama, Fuki M., additional, Holm, Ingrid A., additional, Hom, Jason, additional, Horike-Pyne, Martha, additional, Huang, Alden, additional, Huang, Yan, additional, Hutchison, Sarah, additional, Introne, Wendy, additional, Isasi, Rosario, additional, Izumi, Kosuke, additional, Jarvik, Gail P., additional, Jarvik, Jeffrey, additional, Jayadev, Suman, additional, Jean-Marie, Orpa, additional, Jobanputra, Vaidehi, additional, Kaitryn, Emerald, additional, Ketkar, Shamika, additional, Kiley, Dana, additional, Kilich, Gonench, additional, Kobren, Shilpa N., additional, Kohane, Isaac S., additional, Kohler, Jennefer N., additional, Korrick, Susan, additional, Krakow, Deborah, additional, Krasnewich, Donna M., additional, Kravets, Elijah, additional, Lalani, Seema R., additional, Lam, Byron, additional, Lam, Christina, additional, Lanpher, Brendan C., additional, Lanza, Ian R., additional, LeBlanc, Kimberly, additional, Lee, Brendan H., additional, Levitt, Roy, additional, Lewis, Richard A., additional, Liu, Pengfei, additional, Liu, Xue Zhong, additional, Longo, Nicola, additional, Loo, Sandra K., additional, Loscalzo, Joseph, additional, Maas, Richard L., additional, Macnamara, Ellen F., additional, MacRae, Calum A., additional, Maduro, Valerie V., additional, Maghiro, AudreyStephannie, additional, Mahoney, Rachel, additional, Malicdan, May Christine V., additional, Mamounas, Laura A., additional, Manolio, Teri A., additional, Mao, Rong, additional, Marom, Ronit, additional, Marth, Gabor, additional, Martin, Beth A., additional, Martin, Martin G., additional, Martínez-Agosto, Julian A., additional, Marwaha, Shruti, additional, McCauley, Jacob, additional, McConkie-Rosell, Allyn, additional, McCray, Alexa T., additional, McGee, Elisabeth, additional, Might, Matthew, additional, Miller, Danny, additional, Mirzaa, Ghayda, additional, Morava, Eva, additional, Moretti, Paolo, additional, Morimoto, Marie, additional, Mulvihill, John J., additional, Nakano-Okuno, Mariko, additional, Nelson, Stanley F., additional, Nieves-Rodriguez, Shirley, additional, Novacic, Donna, additional, Oglesbee, Devin, additional, Orengo, James P., additional, Pace, Laura, additional, Pak, Stephen, additional, Pallais, J. Carl, additional, Papp, Jeanette C., additional, Parker, Neil H., additional, Petcharet, Leoyklang, additional, Posey, Jennifer E., additional, Potocki, Lorraine, additional, Swerdzewski, Barbara N. Pusey, additional, Quinlan, Aaron, additional, Rao, Deepak A., additional, Raper, Anna, additional, Raskind, Wendy, additional, Renteria, Genecee, additional, Reuter, Chloe M., additional, Rives, Lynette, additional, Robertson, Amy K., additional, Rodan, Lance H., additional, Rosenthal, Elizabeth, additional, Rossignol, Francis, additional, Ruzhnikov, Maura, additional, Sabaii, Marla, additional, Sacco, Ralph, additional, Sampson, Jacinda B., additional, Saporta, Mario, additional, Schaechter, Judy, additional, Schedl, Timothy, additional, Schoch, Kelly, additional, Scott, Daryl A., additional, Seto, Elaine, additional, Sharma, Prashant, additional, Shashi, Vandana, additional, Shelkowitz, Emily, additional, Sheppeard, Sam, additional, Shin, Jimann, additional, Silverman, Edwin K., additional, Sinsheimer, Janet S., additional, Sisco, Kathy, additional, Smith, Edward C., additional, Smith, Kevin S., additional, Solnica-Krezel, Lilianna, additional, Solomon, Ben, additional, Spillmann, Rebecca C., additional, Stergachis, Andrew, additional, Stoler, Joan M., additional, Sullivan, Kathleen, additional, Sullivan, Jennifer A., additional, Sutton, Shirley, additional, Sweetser, David A., additional, Sybert, Virginia, additional, Tabor, Holly K., additional, Tan, Queenie K.-G., additional, Tan, Amelia L.M., additional, Tarakad, Arjun, additional, Taylor, Herman, additional, Tekin, Mustafa, additional, Telischi, Fred, additional, Thorson, Willa, additional, Tifft, Cynthia J., additional, Toro, Camilo, additional, Tran, Alyssa A., additional, Ungar, Rachel A., additional, Urv, Tiina K., additional, Vanderver, Adeline, additional, Velinder, Matt, additional, Viskochil, Dave, additional, Vogel, Tiphanie P., additional, Wahl, Colleen E., additional, Walker, Melissa, additional, Walley, Nicole M., additional, Wambach, Jennifer, additional, Wan, Jijun, additional, Wang, Lee-kai, additional, Wangler, Michael F., additional, Ward, Patricia A., additional, Wegner, Daniel, additional, Weisz Hubshman, Monika, additional, Wener, Mark, additional, Wenger, Tara, additional, Westerfield, Monte, additional, Wheeler, Matthew T., additional, Whitlock, Jordan, additional, Wolfe, Lynne A., additional, Worley, Kim, additional, Yamamoto, Shinya, additional, Zhang, Zhe, additional, and Zuchner, Stephan, additional
Published: 2024
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7. Loss of function mutations in GEMIN5 cause a neurodevelopmental disorder

Author: Kour, Sukhleen, Rajan, Deepa S., Fortuna, Tyler R., Anderson, Eric N., Ward, Caroline, Lee, Youngha, Lee, Sangmoon, Shin, Yong Beom, Chae, Jong-Hee, Choi, Murim, Siquier, Karine, Cantagrel, Vincent, Amiel, Jeanne, Stolerman, Elliot S., Barnett, Sarah S., Cousin, Margot A., Castro, Diana, McDonald, Kimberly, Kirmse, Brian, Nemeth, Andrea H., Rajasundaram, Dhivyaa, Innes, A. Micheil, Lynch, Danielle, Frosk, Patrick, Collins, Abigail, Gibbons, Melissa, Yang, Michele, Desguerre, Isabelle, Boddaert, Nathalie, Gitiaux, Cyril, Rydning, Siri Lynne, Selmer, Kaja K., Urreizti, Roser, Garcia-Oguiza, Alberto, Osorio, Andrés Nascimento, Verdura, Edgard, Pujol, Aurora, McCurry, Hannah R., Landers, John E., Agnihotri, Sameer, Andriescu, E. Corina, Moody, Shade B., Phornphutkul, Chanika, Sacoto, Maria J. Guillen, Begtrup, Amber, Houlden, Henry, Kirschner, Janbernd, Schorling, David, Rudnik-Schöneborn, Sabine, Strom, Tim M., Leiz, Steffen, Juliette, Kali, Richardson, Randal, Yang, Ying, Zhang, Yuehua, Wang, Minghui, Wang, Jia, Wang, Xiaodong, Platzer, Konrad, Donkervoort, Sandra, Bönnemann, Carsten G., Wagner, Matias, Issa, Mahmoud Y., Elbendary, Hasnaa M., Stanley, Valentina, Maroofian, Reza, Gleeson, Joseph G., Zaki, Maha S., Senderek, Jan, and Pandey, Udai Bhan
Published: 2021
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8. Biallelic mutations in SNX14 cause a syndromic form of cerebellar atrophy and lysosome-autophagosome dysfunction

Author: Akizu, Naiara, Cantagrel, Vincent, Zaki, Maha S, Al-Gazali, Lihadh, Wang, Xin, Rosti, Rasim Ozgur, Dikoglu, Esra, Gelot, Antoinette Bernabe, Rosti, Basak, Vaux, Keith K, Scott, Eric M, Silhavy, Jennifer L, Schroth, Jana, Copeland, Brett, Schaffer, Ashleigh E, Gordts, Philip LSM, Esko, Jeffrey D, Buschman, Matthew D, Field, Seth J, Napolitano, Gennaro, Abdel-Salam, Ghada M, Ozgul, R Koksal, Sagıroglu, Mahmut Samil, Azam, Matloob, Ismail, Samira, Aglan, Mona, Selim, Laila, Mahmoud, Iman G, Abdel-Hadi, Sawsan, Badawy, Amera El, Sadek, Abdelrahim A, Mojahedi, Faezeh, Kayserili, Hulya, Masri, Amira, Bastaki, Laila, Temtamy, Samia, Müller, Ulrich, Desguerre, Isabelle, Casanova, Jean-Laurent, Dursun, Ali, Gunel, Murat, Gabriel, Stacey B, de Lonlay, Pascale, and Gleeson, Joseph G
Subjects: Biological Sciences, Bioinformatics and Computational Biology, Brain Disorders, Clinical Research, Animals, Atrophy, Autophagy, Cerebellar Diseases, Cerebellum, Child, Preschool, Female, Gene Frequency, Humans, Infant, Lod Score, Lysosomal Storage Diseases, Lysosomes, Male, Mutation, Phagosomes, Sorting Nexins, Spinocerebellar Ataxias, Syndrome, Zebrafish, Medical and Health Sciences, Developmental Biology, Agricultural biotechnology, Bioinformatics and computational biology, Genetics
Abstract: Pediatric-onset ataxias often present clinically as developmental delay and intellectual disability, with prominent cerebellar atrophy as a key neuroradiographic finding. Here we describe a new clinically distinguishable recessive syndrome in 12 families with cerebellar atrophy together with ataxia, coarsened facial features and intellectual disability, due to truncating mutations in the sorting nexin gene SNX14, encoding a ubiquitously expressed modular PX domain-containing sorting factor. We found SNX14 localized to lysosomes and associated with phosphatidylinositol (3,5)-bisphosphate, a key component of late endosomes/lysosomes. Patient-derived cells showed engorged lysosomes and a slower autophagosome clearance rate upon autophagy induction by starvation. Zebrafish morphants for snx14 showed dramatic loss of cerebellar parenchyma, accumulation of autophagosomes and activation of apoptosis. Our results characterize a unique ataxia syndrome due to biallelic SNX14 mutations leading to lysosome-autophagosome dysfunction.
Published: 2015

9. LSM7 variants involving key amino acids for LSM complex function cause a neurodevelopmental disorder with leukodystrophy and cerebellar atrophy

Author: Crespin, Matis, Siquier-Pernet, Karine, Marzin, Pauline, Bole-Feysot, Christine, Malan, Valérie, Nitschké, Patrick, Hully, Marie, Roux, Charles-Joris, Lemoine, Michel, Rio, Marlène, Boddaert, Nathalie, Courtin, Thomas, and Cantagrel, Vincent
Published: 2025
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10. CLP1 Founder Mutation Links tRNA Splicing and Maturation to Cerebellar Development and Neurodegeneration

Author: Schaffer, Ashleigh E, Eggens, Veerle RC, Caglayan, Ahmet Okay, Reuter, Miriam S, Scott, Eric, Coufal, Nicole G, Silhavy, Jennifer L, Xue, Yuanchao, Kayserili, Hulya, Yasuno, Katsuhito, Rosti, Rasim Ozgur, Abdellateef, Mostafa, Caglar, Caner, Kasher, Paul R, Cazemier, J Leonie, Weterman, Marian A, Cantagrel, Vincent, Cai, Na, Zweier, Christiane, Altunoglu, Umut, Satkin, N Bilge, Aktar, Fesih, Tuysuz, Beyhan, Yalcinkaya, Cengiz, Caksen, Huseyin, Bilguvar, Kaya, Fu, Xiang-Dong, Trotta, Christopher R, Gabriel, Stacey, Reis, André, Gunel, Murat, Baas, Frank, and Gleeson, Joseph G
Subjects: Biochemistry and Cell Biology, Biomedical and Clinical Sciences, Biological Sciences, Neurodegenerative, Genetics, Neurosciences, Aetiology, 2.1 Biological and endogenous factors, Generic health relevance, Neurological, Animals, Brain, Cerebellum, Cleavage And Polyadenylation Specificity Factor, Female, Humans, Male, Mice, Models, Molecular, Neurodegenerative Diseases, Nuclear Proteins, Pedigree, Phosphotransferases, RNA Splicing, RNA, Transfer, Saccharomyces cerevisiae, Transcription Factors, Zebrafish, Zebrafish Proteins, Medical and Health Sciences, Developmental Biology, Biological sciences, Biomedical and clinical sciences
Abstract: Neurodegenerative diseases can occur so early as to affect neurodevelopment. From a cohort of more than 2,000 consanguineous families with childhood neurological disease, we identified a founder mutation in four independent pedigrees in cleavage and polyadenylation factor I subunit 1 (CLP1). CLP1 is a multifunctional kinase implicated in tRNA, mRNA, and siRNA maturation. Kinase activity of the CLP1 mutant protein was defective, and the tRNA endonuclease complex (TSEN) was destabilized, resulting in impaired pre-tRNA cleavage. Germline clp1 null zebrafish showed cerebellar neurodegeneration that was rescued by wild-type, but not mutant, human CLP1 expression. Patient-derived induced neurons displayed both depletion of mature tRNAs and accumulation of unspliced pre-tRNAs. Transfection of partially processed tRNA fragments into patient cells exacerbated an oxidative stress-induced reduction in cell survival. Our data link tRNA maturation to neuronal development and neurodegeneration through defective CLP1 function in humans.
Published: 2014

11. Supernumerary chromosome 6 marker associated with paternal uniparental isodisomy of chromosome 6 in a patient with a syndromic disorder of insulin secretion

Author: Lesieur-Sebellin, Marion, primary, Marzin, Pauline, additional, Arnoux, Jean-Baptiste, additional, Maurin, Marie-Laure, additional, Receveur, Aline, additional, Cantagrel, Vincent, additional, Rose, Sylvia, additional, Dorval, Guillaume, additional, Levy, Jonathan, additional, and Malan, Valérie, additional
Published: 2023
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12. MINPP1 prevents intracellular accumulation of the chelator inositol hexakisphosphate and is mutated in Pontocerebellar Hypoplasia

Author: Ucuncu, Ekin, Rajamani, Karthyayani, Wilson, Miranda S. C., Medina-Cano, Daniel, Altin, Nami, David, Pierre, Barcia, Giulia, Lefort, Nathalie, Banal, Céline, Vasilache-Dangles, Marie-Thérèse, Pitelet, Gaële, Lorino, Elsa, Rabasse, Nathalie, Bieth, Eric, Zaki, Maha S., Topcu, Meral, Sonmez, Fatma Mujgan, Musaev, Damir, Stanley, Valentina, Bole-Feysot, Christine, Nitschké, Patrick, Munnich, Arnold, Bahi-Buisson, Nadia, Fossoud, Catherine, Giuliano, Fabienne, Colleaux, Laurence, Burglen, Lydie, Gleeson, Joseph G., Boddaert, Nathalie, Saiardi, Adolfo, and Cantagrel, Vincent
Published: 2020
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13. Association d’un marqueur surnuméraire et d’une isodisomie uniparentale paternelle du chromosome 6 chez un patient présentant un retard de développement syndromique

Author: Lesieur-Sebellin, Marion, Marzin, Pauline, Arnoux, Jean-Baptiste, Maurin, Marie-Laure, Receveur, Aline, Cantagrel, Vincent, Rose, Sylvia, Dorval, Guillaume, Levy, Jonathan, and Malan, Valérie
Published: 2023
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14. Recurrent KIF5C mutation leading to frontal pachygyria without microcephaly

Author: Cavallin, Mara, Hubert, Laurence, Cantagrel, Vincent, Munnich, Arnold, Boddaert, Nathalie, Vincent-Delorme, Catherine, Cuvellier, Jean Christophe, Masson, Cecile, Besmond, Claude, and Bahi-Buisson, Nadia
Published: 2016
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15. Biallelic loss of EMC10 leads to mild to severe intellectual disability

Author: Kaiyrzhanov, Rauan, primary, Rocca, Clarissa, additional, Suri, Mohnish, additional, Gulieva, Sughra, additional, Zaki, Maha S., additional, Henig, Noa Z., additional, Siquier, Karine, additional, Guliyeva, Ulviyya, additional, Mounir, Samir M., additional, Marom, Daphna, additional, Allahverdiyeva, Aynur, additional, Megahed, Hisham, additional, van Bokhoven, Hans, additional, Cantagrel, Vincent, additional, Rad, Aboulfazl, additional, Pourkeramti, Alemeh, additional, Dehghani, Boshra, additional, Shao, Diane D., additional, Markus‐Bustani, Keren, additional, Sofrin‐Drucker, Efrat, additional, Orenstein, Naama, additional, Salayev, Kamran, additional, Arrigoni, Filippo, additional, Houlden, Henry, additional, and Maroofian, Reza, additional
Published: 2022
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16. WDR81 mutations cause extreme microcephaly and impair mitotic progression in human fibroblasts and Drosophila neural stem cells

Author: Cavallin, Mara, Rujano, Maria A., Bednarek, Nathalie, Medina-Cano, Daniel, Bernabe Gelot, Antoinette, Drunat, Severine, Maillard, Camille, Garfa-Traore, Meriem, Bole, Christine, Nitschké, Patrick, Beneteau, Claire, Besnard, Thomas, Cogné, Benjamin, Eveillard, Marion, Kuster, Alice, Poirier, Karine, Verloes, Alain, Martinovic, Jelena, Bidat, Laurent, Rio, Marlene, Lyonnet, Stanislas, Reilly, M. Louise, Boddaert, Nathalie, Jenneson-Liver, Melanie, Motte, Jacques, Doco-Fenzy, Martine, Chelly, Jamel, Attie-Bitach, Tania, Simons, Matias, Cantagrel, Vincent, Passemard, Sandrine, Baffet, Alexandre, Thomas, Sophie, and Bahi-Buisson, Nadia
Published: 2017
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17. Suleiman-El-Hattab syndrome: a histone modification disorder caused by TASP1 deficiency

Author: Riedhammer, Korbinian M, primary, Burgemeister, Anna L, additional, Cantagrel, Vincent, additional, Amiel, Jeanne, additional, Siquier-Pernet, Karine, additional, Boddaert, Nathalie, additional, Hertecant, Jozef, additional, Kannouche, Patricia L, additional, Pouvelle, Caroline, additional, Htun, Stephanie, additional, Slavotinek, Anne M, additional, Beetz, Christian, additional, Diego-Alvarez, Dan, additional, Kampe, Kapil, additional, Fleischer, Nicole, additional, Awamleh, Zain, additional, Weksberg, Rosanna, additional, Kopajtich, Robert, additional, Meitinger, Thomas, additional, Suleiman, Jehan, additional, and El-Hattab, Ayman W, additional
Published: 2022
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18. Recessive PRDM13 mutations cause fatal perinatal brainstem dysfunction with cerebellar hypoplasia and disrupt Purkinje cell differentiation

Author: Coolen, Marion, primary, Altin, Nami, additional, Rajamani, Karthyayani, additional, Pereira, Eva, additional, Siquier-Pernet, Karine, additional, Puig Lombardi, Emilia, additional, Moreno, Nadjeda, additional, Barcia, Giulia, additional, Yvert, Marianne, additional, Laquerrière, Annie, additional, Pouliet, Aurore, additional, Nitschké, Patrick, additional, Boddaert, Nathalie, additional, Rausell, Antonio, additional, Razavi, Féréchté, additional, Afenjar, Alexandra, additional, Billette de Villemeur, Thierry, additional, Al-Maawali, Almundher, additional, Al-Thihli, Khalid, additional, Baptista, Julia, additional, Beleza-Meireles, Ana, additional, Garel, Catherine, additional, Legendre, Marine, additional, Gelot, Antoinette, additional, Burglen, Lydie, additional, Moutton, Sébastien, additional, and Cantagrel, Vincent, additional
Published: 2022
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19. Mild phenotype of Molybdenum cofactor (MoCo) deficiency Type B among Egyptian patients

Author: Megahed, Hisham, primary, Ashaat, Engy, additional, Ismail, Samira, additional, Ashaat, Neveen, additional, Cantagrel, Vincent, additional, and El Ruby, Mona, additional
Published: 2022
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20. Terminal 6q deletions cause brain malformations, a phenotype mimicking heterozygous DLL1 pathogenic variants: A multicenter retrospective case series

Author: Lesieur‐Sebellin, Marion, primary, Till, Marianne, additional, Khau Van Kien, Philippe, additional, Herve, Bérénice, additional, Bourgon, Nicolas, additional, Dupont, Céline, additional, Tabet, Anne‐Claude, additional, Barrois, Mathilde, additional, Coussement, Aurélie, additional, Loeuillet, Laurence, additional, Mousty, Eve, additional, Ea, Vuthy, additional, Assal, Amal, additional, Mary, Laura, additional, Jaillard, Sylvie, additional, Beneteau, Claire, additional, Le Vaillant, Claudine, additional, Coutton, Charles, additional, Devillard, Françoise, additional, Goumy, Carole, additional, Delabaere, Amélie, additional, Redon, Sylvia, additional, Laurent, Yves, additional, Lamouroux, Audrey, additional, Massardier, Jérôme, additional, Turleau, Catherine, additional, Sanlaville, Damien, additional, Cantagrel, Vincent, additional, Sonigo, Pascale, additional, Vialard, François, additional, Salomon, Laurent J., additional, and Malan, Valérie, additional
Published: 2021
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21. Emm : un nouveau système de groupe sanguin associé à des troubles neurodéveloppementaux

Author: Duval, Romain, primary, Nicolas, Gael, additional, Willemetz, Alexandra, additional, Murakami, Yoshiko, additional, Mikdar, Mahmoud, additional, Vrignaud, Cedric, additional, Megahed, Hisham, additional, Cartron, Jean-Pierre, additional, Masson, Cecile, additional, Wehbi, Samer, additional, Koehl, Bérengere, additional, Hully, Marie, additional, Siquier, Karine, additional, Chemlay, Nicole, additional, Rotig, Agnes, additional, Lyonnet, Stanislas, additional, Colin, Yves, additional, Barcia, Giulia, additional, Cantagrel, Vincent, additional, Le Van Kim, Caroline, additional, Hermine, Olivier, additional, Kinoshita, Taroh, additional, Peyrard, Thierry, additional, and Azouzi, Slim, additional
Published: 2021
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22. Une hypoplasie ponto-cérébelleuse causée par l’accumulation d’un inositol phosphate

Author: Ucuncu, Ekin, primary, Rajamani, Karthyayani, additional, Burglen, Lydie, additional, Boddaert, Nathalie, additional, Saiardi, Adolfo, additional, and Cantagrel, Vincent, additional
Published: 2021
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23. From glycosylation disorders to dolichol biosynthesis defects: a new class of metabolic diseases

Author: Cantagrel, Vincent and Lefeber, Dirk J.
Published: 2011
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24. Inherited glycosylphosphatidylinositol defects cause the rare Emm-negative blood phenotype and developmental disorders

Author: Duval, Romain, primary, Nicolas, Gaël, additional, Willemetz, Alexandra, additional, Murakami, Yoshiko, additional, Mikdar, Mahmoud, additional, Vrignaud, Cedric, additional, Megahed, Hisham, additional, Cartron, Jean-Pierre, additional, Masson, Cecile, additional, Wehbi, Samer, additional, Koehl, Bérengere, additional, Hully, Marie, additional, Siquier, Karine, additional, Chemlay, Nicole, additional, Rotig, Agnes, additional, Lyonnet, Stanislas, additional, Colin, Yves, additional, Barcia, Giulia, additional, Cantagrel, Vincent, additional, Le Van Kim, Caroline, additional, Hermine, Olivier, additional, Kinoshita, Taroh, additional, Peyrard, Thierry, additional, and Azouzi, Slim, additional
Published: 2021
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25. Mutations in the cilia gene ARL13B lead to the classical form of Joubert syndrome

Author: Cantagrel, Vincent, Silhavy, Jennifer L., Bielas, Stephanie L., Swistun, Dominika, Marsh, Sarah E., Bertrand, Julien Y., Audollent, Sophie, Attie-Bitach, Tania, Holden, Kenton R., Dobyns, William B., Traver, David, Al-Gazali, Lihadh, Ali, Bassam R., Linder, Tom H., Caspary, Tamara, Otto, Edgar A., Hildebrandt, Friedhelm, Glass, Ian A., Logan, Clare V., Johnson, Colin A., Bennett, Christopher, Brancati, Francesco, Valente, Enza Maria, Woods, C. Geoffrey, and Gleeson, Joseph G.
Subjects: Cilia and ciliary motion -- Genetic aspects, Gene expression -- Analysis, Gene mutations -- Analysis, Joubert syndrome -- Genetic aspects, Biological sciences
Abstract: The mutations in the cilia gene ARL13B present in two different families suffering from the classical form of the Joubert syndrome (JS) are studied. The encoded protein is shown to be expressed in the developing murine cerebellum and plays an extremely significant role in mediating the cilia function in multiple organs.
Published: 2008

26. MINPP1prevents intracellular accumulation of the cation chelator inositol hexakisphosphate and is mutated in Pontocerebellar Hypoplasia

Author: Ucuncu, Ekin, primary, Rajamani, Karthyayani, additional, Wilson, Miranda S.C., additional, Medina-Cano, Daniel, additional, Altin, Nami, additional, David, Pierre, additional, Barcia, Giulia, additional, Lefort, Nathalie, additional, Vasilache-Dangles, Marie-Thérèse, additional, Pitelet, Gaële, additional, Lorino, Elsa, additional, Rabasse, Nathalie, additional, Bieth, Eric, additional, Zaki, Maha S., additional, Topcu, Meral, additional, Sonmez, Fatma Mujgan, additional, Musaev, Damir, additional, Stanley, Valentina, additional, Bole-Feysot, Christine, additional, Nitschké, Patrick, additional, Munnich, Arnold, additional, Bahi-Buisson, Nadia, additional, Fossoud, Catherine, additional, Giuliano, Fabienne, additional, Colleaux, Laurence, additional, Burglen, Lydie, additional, Gleeson, Joseph G., additional, Boddaert, Nathalie, additional, Saiardi, Adolfo, additional, and Cantagrel, Vincent, additional
Published: 2020
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27. Opposite Modulation of RAC1 by Mutations in TRIO Is Associated with Distinct, Domain-Specific Neurodevelopmental Disorders

Author: Barbosa, Sónia, primary, Greville-Heygate, Stephanie, additional, Bonnet, Maxime, additional, Godwin, Annie, additional, Fagotto-Kaufmann, Christine, additional, Kajava, Andrey V., additional, Laouteouet, Damien, additional, Mawby, Rebecca, additional, Wai, Htoo Aung, additional, Dingemans, Alexander J.M., additional, Hehir-Kwa, Jayne, additional, Willems, Marjorlaine, additional, Capri, Yline, additional, Mehta, Sarju G., additional, Cox, Helen, additional, Goudie, David, additional, Vansenne, Fleur, additional, Turnpenny, Peter, additional, Vincent, Marie, additional, Cogné, Benjamin, additional, Lesca, Gaëtan, additional, Hertecant, Jozef, additional, Rodriguez, Diana, additional, Keren, Boris, additional, Burglen, Lydie, additional, Gérard, Marion, additional, Putoux, Audrey, additional, Cantagrel, Vincent, additional, Siquier-Pernet, Karine, additional, Rio, Marlene, additional, Banka, Siddharth, additional, Sarkar, Ajoy, additional, Steeves, Marcie, additional, Parker, Michael, additional, Clement, Emma, additional, Moutton, Sébastien, additional, Tran Mau-Them, Frédéric, additional, Piton, Amélie, additional, de Vries, Bert B.A., additional, Guille, Matthew, additional, Debant, Anne, additional, Schmidt, Susanne, additional, and Baralle, Diana, additional
Published: 2020
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28. A novel cerebello-ocular syndrome with abnormal glycosylation due to abnormalities in dolichol metabolism

Author: Morava, Eva, Wevers, Ron A., Cantagrel, Vincent, Hoefsloot, Lies H., Al-Gazali, Lihadh, Schoots, Jeroen, van Rooij, Arno, Huijben, Karin, van Ravenswaaij-Arts, Connie M. A., Jongmans, Marjolein C. J., Sykut-Cegielska, Jolanta, Hoffmann, Georg F., Bluemel, Peter, Adamowicz, Maciej, van Reeuwijk, Jeroen, Ng, Bobby G., Bergman, Jorieke E. H., van Bokhoven, Hans, Körner, Christian, Babovic-Vuksanovic, Dusica, Willemsen, Michel A., Gleeson, Joseph G., Lehle, Ludwig, de Brouwer, Arjan P. M., and Lefeber, Dirk J.
Published: 2010
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29. Fetal bovine serum impacts the observed N‐glycosylation defects in TMEM165 KO HEK cells

Author: Climer, Leslie, Morelle, Willy, De Bettignies, Geoffroy, Krzewinski Recchi, Marie-Ange, Lupashin, Vladimir, Medina-Cano, Daniel, Ucuncu, Ekin, Nguyen, Lam Son, Nicouleau, Michael, Lipecka, Joanna, Bizot, Jean-Charles, Thiel, Christian, Lefort, Nathalie, Faivre-Sarrailh, Catherine, Colleaux, Laurence, Guerrera, Ida Chiara, Cantagrel, Vincent, Lebredonchel, Elodie, Garat, Anne, Legrand, Dominique, Decool, Valérie, Klein, André, Ouzzine, Mohamed, Gasnier, Bruno, Potelle, Sven, Groux‐Degroote, Sophie, Cogez, Virginie, Noel, Maxence, Portier, Lucie, Solórzano, Carlos, Dall'Olio, Fabio, Steenackers, Agata, Mortuaire, Marlène, Gonzalez‐Pisfil, Mariano, Henry, Mélanie, Heliot, Laurent, Harduin-Lepers, Anne, Berthe, Audrey, Zaffino, Marie, Muller, claire, Houdou, Marine, Schulz, Céline, Bost, Frédéric, De Fay, Elia, Mazerbourg, Sabine, Flament, Stéphane, Mouajjah, Dounia, Ashikov, Angel, Abu Bakar, Nurulamin, Wen, Xiao-Yan, Niemeijer, Marco, Rodrigues Pinto Osorio, Glentino, Brand-Arzamendi, Koroboshka, Hasadsri, Linda, Hansikova, Hana, Raymond, Kimiyo, Ondruskova, Nina, Simon, Marleen, Pfundt, Rolph, Timal, Sharita, Beumers, Roel, Smeets, Roel, Kersten, Marjan, Huijben, Karin, Linders, Peter, van den Bogaart, Geert, van Hijum, Sacha, Rodenburg, Richard, van den Heuvel, Lambertus, Van Spronsen, Francjan, Honzik, Tomas, van Scherpenzeel, Monique, Lefeber, Dirk, Mirjam, Wamelink, Han, Brunner, Helen, Mundy, Helen, Michelakakis, Peter, van Hasselt, Jiddeke, van de Kamp, Diego, Martinelli, Lars, Morkrid, Katja, Brocke Holmefjord, Jozef, Hertecant, Majid, Alfadhel, Kevin, Carpenter, Johann, te Water Naude, Delos, Maxime, Hellec, Charles, Fifre, Alexandre, Carpentier, Mathieu, Papy-Garcia, Dulce, Allain, Fabrice, Denys, Agnés, Gilormini, Pierre André, Lion, Cédric, Vicogne, Dorothée, Guerardel, Yann, Biot, Christophe, Witters, Peter, Breckpot, Jeroen, Preston, Graem, Morava, Eva, Rujano, Maria, Cannata Serio, Magda, Panasyuk, Ganna, Reunert, Janine, Hauser, Virginie, Park, Julien, Freisinger, Peter, Guida, Maria Clara, Maier, Esther, Wada, Yoshinao, Jäger, Stefanie, Krogan, Nevan, Kretz, Oliver, Nobre, Susana, Garcia, Paula, Quelhas, Dulce, Bird, Thomas, Raskind, Wendy, Schwake, Michael, Duvet, Sandrine, Marquardt, Thorsten, Simons, Matias, Blommaert, Eline, Péanne, Romain, Cherepanova, Natalia, Rymen, Daisy, Staels, Frederik, Jaeken, Jaak, Race, Valérie, Keldermans, Liesbeth, Souche, Erika, Corveleyn, Anniek, Sparkes, Rebecca, Bhattacharya, Kaustuv, Devalck, Christine, Schrijvers, Rik, Foulquier, Francois, Gilmore, Reid, Matthijs, Gert, Université Lille Nord de France (COMUE), Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 (UGSF), Université de Lille-Centre National de la Recherche Scientifique (CNRS), Variabilité génétique des défenses de l'organisme face à son environnement chimique, PRES Université Lille Nord de France-Université de Lille, Droit et Santé, ANR-15-CE14-0001,SOLV_CDG,Décryptage des patients CDG (Congenital Disorders of Glyvosylation) déficients en TMEM165 - de la compréhension des mécanismes moléculaires à une thérapie(2015), ANR-15-RAR3-0004,EURO-CDG-2,A European research network directed towards improving diagnosis and treatment of inborn glycosylation disorders.(2015), European Project: 643578,H2020,H2020-HCO-2014,E-Rare-3(2014), Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 (UGSF), Université de Lille-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Recherche Agronomique (INRA), Institut National de la Recherche Agronomique (INRA)-Université de Lille-Centre National de la Recherche Scientifique (CNRS), Université de Lille, CNRS, Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 [UGSF], Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF], Centre Hospitalier Régional Universitaire [Lille] [CHRU Lille], Impact de l'environnement chimique sur la santé humaine - ULR 4483 [IMPECS], Baylor University, University of Arkansas for Medical Sciences [UAMS], Institut de Génétique Moléculaire de Montpellier (IGMM), Centre National de la Recherche Scientifique (CNRS)-Université de Montpellier (UM), Imagine - Institut des maladies génétiques (IMAGINE - U1163), Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Institut de psychiatrie et neurosciences (U894 / UMS 1266), Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM), Key-Obs, JRC Institute for Energy and Transport (IET), European Commission - Joint Research Centre [Petten], Institut de Neurobiologie de la Méditerranée [Aix-Marseille Université] (INMED - INSERM U1249), Aix Marseille Université (AMU)-Institut National de la Santé et de la Recherche Médicale (INSERM), Plateforme Protéomique Necker [SFR Necker] (PPN - 3P5), Structure Fédérative de Recherche Necker (SFR Necker - UMS 3633 / US24), Assistance publique - Hôpitaux de Paris (AP-HP) (APHP)-Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Assistance publique - Hôpitaux de Paris (AP-HP) (APHP)-Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Impact de l'environnement chimique sur la santé humaine (IMPECS), Centre Hospitalier Régional Universitaire [Lille] (CHRU Lille)-Université de Lille, Biologie cellulaire et moléculaire de la sécrétion (BCMS), Centre National de la Recherche Scientifique (CNRS), Departamento de Bioquímica, Instituto Nacional de Enfermedades Respiratorias, Department of Experimental, Diagnostic and Specialty Medicine (DIMES) (DIMES), Università di Bologna [Bologna] (UNIBO), Laboratoire de Physique des Lasers, Atomes et Molécules - UMR 8523 (PhLAM), Biophotonique Cellulaire Fonctionelle, Institut de Recherche Interdisciplinaire, Institut de Recherche Interdisciplinaire [Villeneuve d'Ascq] (IRI), Université de Lille, Sciences et Technologies-Université de Lille, Droit et Santé-Centre National de la Recherche Scientifique (CNRS), Centre méditerranéen de médecine moléculaire (C3M), Université Nice Sophia Antipolis (UNS), Université Côte d'Azur (UCA)-Université Côte d'Azur (UCA)-Institut National de la Santé et de la Recherche Médicale (INSERM), Department of Medicine & Physiology , University of Toronto, First Faculty of Medicine, Charles University [Prague], University Medical Center [Utrecht], Department of Human Genetics, Radboud University Medical Center [Nijmegen], Paediatrics, Beatrix Children's Hospital/University Medical Center Groningen, Université Toulouse 1 Capitole (UT1), Croissance cellulaire, réparation et régénération tissulaires (CRRET), Université Paris-Est Créteil Val-de-Marne - Paris 12 (UPEC UP12)-Centre National de la Recherche Scientifique (CNRS), Chimie Moléculaire et Formulation (EA 4478), Université de Lille, Sciences et Technologies, Unité de Catalyse et de Chimie du Solide - UMR 8181 (UCCS), Université d'Artois (UA)-Ecole Centrale de Lille-Ecole Nationale Supérieure de Chimie de Lille (ENSCL)-Université de Lille-Centre National de la Recherche Scientifique (CNRS), Department of Pediatrics, University Children's Hospital, Centre de recherche Croissance et signalisation (UMR_S 845), Reutlingen University, Department of General Pediatrics, Münster University Children Hospital, Molecular Diagnostics, Center for Human Genetics, Gasthuisberg, Katholieke Universiteit Leuven and Flanders Interuniversity Institute for Biotechnology 4, Leuven, Belgium, Catholic University of Leuven - Katholieke Universiteit Leuven (KU Leuven), Center for Human Genetics, and Laboratory of clinical immunology
Subjects: Glycosylation, Protein family, [SDV]Life Sciences [q-bio], Golgi Apparatus, FBS, manganese level, N‐glycosylation defects, TMEM165, Article, Antiporters, Glycomics, 03 medical and health sciences, chemistry.chemical_compound, symbols.namesake, Congenital Disorders of Glycosylation, 0302 clinical medicine, N-linked glycosylation, Genetics, Humans, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biochemistry [q-bio.BM], Cation Transport Proteins, Genetics (clinical), ComputingMilieux_MISCELLANEOUS, 030304 developmental biology, Manganese, 0303 health sciences, Ion Transport, HEK 293 cells, Serum Albumin, Bovine, Golgi apparatus, Embryonic stem cell, Cell biology, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biomolecules [q-bio.BM], carbohydrates (lipids), HEK293 Cells, chemistry, symbols, Calcium, 030217 neurology & neurosurgery, Fetal bovine serum
Abstract: TMEM165 is involved in a rare genetic human disease named TMEM165‐CDG (congenital disorders of glycosylation). It is Golgi localized, highly conserved through evolution and belongs to the uncharacterized protein family 0016 (UPF0016). The use of isogenic TMEM165 KO HEK cells was crucial in deciphering the function of TMEM165 in Golgi manganese homeostasis. Manganese is a major cofactor of many glycosylation enzymes. Severe Golgi glycosylation defects are observed in TMEM165 Knock Out Human Embryonic Kidney (KO HEK) cells and are rescued by exogenous manganese supplementation. Intriguingly, we demonstrate in this study that the observed Golgi glycosylation defect mainly depends on fetal bovine serum, particularly its manganese level. Our results also demonstrate that iron and/or galactose can modulate the observed glycosylation defects in TMEM165 KO HEK cells. While isogenic cultured cells are widely used to study the impact of gene defects on proteins' glycosylation patterns, these results emphasize the importance of the use of validated fetal bovine serum in glycomics studies. 43;2
Published: 2019

30. Truncation of NHEJ1 in a Patient With Polymicrogyria

Author: Cantagrel, Vincent, Lossi, Anne-Marie, Lisgo, Steven, Missirian, Chantal, Borges, Ana, Philip, Nicole, Fernandez, Carla, Cardoso, Carlos, Figarella-Branger, Dominique, Moncla, Anne, Lindsay, Susan, Dobyns, William B., and Villard, Laurent
Published: 2007
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31. High N-glycan multiplicity is critical for neuronal adhesion and sensitizes the developing cerebellum to N-glycosylation defect

Author: Medina-Cano, Daniel, Ucuncu, Ekin, Nguyen, Lam Son, Nicouleau, Michael, Lipecka, Joanna, Bizot, Jean-Charles, Thiel, Christian, Foulquier, François, Lefort, Nathalie, Faivre-Sarrailh, Catherine, Colleaux, Laurence, Guerrera, Ida Chiara, Cantagrel, Vincent, Imagine - Institut des maladies génétiques (IMAGINE - U1163), Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM), Institut de chimie et procédés pour l'énergie, l'environnement et la santé (ICPEES), Université de Strasbourg (UNISTRA)-Matériaux et nanosciences d'Alsace (FMNGE), Institut de Chimie du CNRS (INC)-Université de Strasbourg (UNISTRA)-Université de Haute-Alsace (UHA) Mulhouse - Colmar (Université de Haute-Alsace (UHA))-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie du CNRS (INC)-Université de Strasbourg (UNISTRA)-Université de Haute-Alsace (UHA) Mulhouse - Colmar (Université de Haute-Alsace (UHA))-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), CHU Trousseau [APHP], Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Sorbonne Université (SU), JRC Institute for Energy and Transport (IET), European Commission - Joint Research Centre [Petten], Institut de Neurobiologie de la Méditerranée [Aix-Marseille Université] (INMED - INSERM U1249), Institut National de la Santé et de la Recherche Médicale (INSERM)-Aix Marseille Université (AMU), Structure Fédérative de Recherche Necker (SFR Necker - UMS 3633 / US24), Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Paris Descartes - Paris 5 (UPD5)-Centre National de la Recherche Scientifique (CNRS), Centre National de la Recherche Scientifique (CNRS)-Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM), Université de Strasbourg (UNISTRA)-Centre National de la Recherche Scientifique (CNRS)-Matériaux et nanosciences d'Alsace, Université de Strasbourg (UNISTRA)-Université de Haute-Alsace (UHA) Mulhouse - Colmar (Université de Haute-Alsace (UHA))-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université de Strasbourg (UNISTRA)-Université de Haute-Alsace (UHA) Mulhouse - Colmar (Université de Haute-Alsace (UHA))-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Aix Marseille Université (AMU)-Institut National de la Santé et de la Recherche Médicale (INSERM), Centre National de la Recherche Scientifique (CNRS)-Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Assistance publique - Hôpitaux de Paris (AP-HP) (APHP), PRA, Fanny, Mécanismes développementaux des anomalies structurelles cérébelleuses - - SCD-Mec2016 - ANR-16-CE12-0005 - AAPG2016 - VALID, ERA-NET rare disease research implementing IRDiRC objectives - E-Rare-3 - - H20202014-12-01 - 2019-11-30 - 643578 - VALID, Institut de psychiatrie et neurosciences (U894 / UMS 1266), Key-Obs, ANR-16-CE12-0005,SCD-Mec,Mécanismes développementaux des anomalies structurelles cérébelleuses(2016), European Project: 643578,H2020,H2020-HCO-2014,E-Rare-3(2014), Université de Strasbourg (UNISTRA)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Matériaux et Nanosciences Grand-Est (MNGE), Université de Strasbourg (UNISTRA)-Université de Haute-Alsace (UHA) Mulhouse - Colmar (Université de Haute-Alsace (UHA))-Institut National de la Santé et de la Recherche Médicale (INSERM)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université de Strasbourg (UNISTRA)-Université de Haute-Alsace (UHA) Mulhouse - Colmar (Université de Haute-Alsace (UHA))-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 (UGSF), Institut National de la Recherche Agronomique (INRA)-Centre National de la Recherche Scientifique (CNRS)-Université de Lille, Centre de recherche en neurobiologie - neurophysiologie de Marseille (CRN2M), Aix Marseille Université (AMU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Université Sorbonne Paris Cité (USPC), and Centre de Psychiatrie et Neurosciences (U894)
Subjects: Glycosylation, MESH: Immunoglobulins, [SDV]Life Sciences [q-bio], MESH: Neurons, N-glycosylation, MESH: Unfolded Protein Response, MESH: Mice, Knockout, neuroscience, Purkinje Cells, MESH: Axon Guidance, Neural Pathways, cell biology, MESH: Animals, Biology (General), Mice, Knockout, Neurons, neuronal migration, MESH: Proteomics, Srd5a3, Cell Differentiation, MESH: Glycosylation, MESH: Motor Activity, Axon Guidance, MESH: Reproducibility of Results, MESH: Cell Adhesion Molecules, Medicine, lipids (amino acids, peptides, and proteins), [SDV.NEU]Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC], MESH: Membrane Proteins, Research Article, MESH: Cell Differentiation, MESH: Mutation, animal structures, cerebellum, QH301-705.5, Science, Induced Pluripotent Stem Cells, Immunoglobulins, MESH: Cytoplasmic Granules, Motor Activity, MESH: Induced Pluripotent Stem Cells, Cytoplasmic Granules, MESH: 3-Oxo-5-alpha-Steroid 4-Dehydrogenase, MESH: Cell Adhesion, MESH: Purkinje Cells, proteomics, 3-Oxo-5-alpha-Steroid 4-Dehydrogenase, Polysaccharides, Animals, human, [SDV.NEU] Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC], mouse, MESH: Neural Pathways, Cell Membrane, Membrane Proteins, Reproducibility of Results, cell adhesion, MESH: Cerebellum, carbohydrates (lipids), MESH: Polysaccharides, [SDV.GEN.GH]Life Sciences [q-bio]/Genetics/Human genetics, MESH: Gene Deletion, Protein N-glycosylation, Mutation, Unfolded Protein Response, Cell Adhesion Molecules, Gene Deletion, MESH: Cell Membrane, congenital disorders of glycosylation
Abstract: International audience; Proper brain development relies highly on protein N-glycosylation to sustain neuronal migration, axon guidance and synaptic physiology. Impairing the N-glycosylation pathway at early steps produces broad neurological symptoms identified in congenital disorders of glycosylation. However, little is known about the molecular mechanisms underlying these defects. We generated a cerebellum specific knockout mouse for Srd5a3, a gene involved in the initiation of N-glycosylation. In addition to motor coordination defects and abnormal granule cell development, Srd5a3 deletion causes mild N-glycosylation impairment without significantly altering ER homeostasis. Using proteomic approaches, we identified that Srd5a3 loss affects a subset of glycoproteins with high N-glycans multiplicity per protein and decreased protein abundance or N-glycosylation level. As IgSF-CAM adhesion proteins are critical for neuron adhesion and highly N-glycosylated, we observed impaired IgSF-CAM-mediated neurite outgrowth and axon guidance in Srd5a3 mutant cerebellum. Our results link high N-glycan multiplicity to fine-tuned neural cell adhesion during mammalian brain development.
Published: 2018

32. Author response: High N-glycan multiplicity is critical for neuronal adhesion and sensitizes the developing cerebellum to N-glycosylation defect

Author: Medina-Cano, Daniel, primary, Ucuncu, Ekin, additional, Nguyen, Lam Son, additional, Nicouleau, Michael, additional, Lipecka, Joanna, additional, Bizot, Jean-Charles, additional, Thiel, Christian, additional, Foulquier, François, additional, Lefort, Nathalie, additional, Faivre-Sarrailh, Catherine, additional, Colleaux, Laurence, additional, Guerrera, Ida Chiara, additional, and Cantagrel, Vincent, additional
Published: 2018
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33. De novo mutation screening in childhood-onset cerebellar atrophy identifies gain-of-function mutations in the CACNA1G calcium channel gene

Author: Chemin, Jean, primary, Siquier-Pernet, Karine, additional, Nicouleau, Michaël, additional, Barcia, Giulia, additional, Ahmad, Ali, additional, Medina-Cano, Daniel, additional, Hanein, Sylvain, additional, Altin, Nami, additional, Hubert, Laurence, additional, Bole-Feysot, Christine, additional, Fourage, Cécile, additional, Nitschké, Patrick, additional, Thevenon, Julien, additional, Rio, Marlène, additional, Blanc, Pierre, additional, vidal, Céline, additional, Bahi-Buisson, Nadia, additional, Desguerre, Isabelle, additional, Munnich, Arnold, additional, Lyonnet, Stanislas, additional, Boddaert, Nathalie, additional, Fassi, Emily, additional, Shinawi, Marwan, additional, Zimmerman, Holly, additional, Amiel, Jeanne, additional, Faivre, Laurence, additional, Colleaux, Laurence, additional, Lory, Philippe, additional, and Cantagrel, Vincent, additional
Published: 2018
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34. Utility of whole exome sequencing for the early diagnosis of pediatric-onset cerebellar atrophy associated with developmental delay in an inbred population

Author: Megahed, Hisham, primary, Nicouleau, Michaël, additional, Barcia, Giulia, additional, Medina-Cano, Daniel, additional, Siquier-Pernet, Karine, additional, Bole-Feysot, Christine, additional, Parisot, Mélanie, additional, Masson, Cécile, additional, Nitschké, Patrick, additional, Rio, Marlène, additional, Bahi-Buisson, Nadia, additional, Desguerre, Isabelle, additional, Munnich, Arnold, additional, Boddaert, Nathalie, additional, Colleaux, Laurence, additional, and Cantagrel, Vincent, additional
Published: 2016
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35. Disruption of POGZ Is Associated with Intellectual Disability and Autism Spectrum Disorders

Author: Stessman, Holly A.F., primary, Willemsen, Marjolein H., additional, Fenckova, Michaela, additional, Penn, Osnat, additional, Hoischen, Alexander, additional, Xiong, Bo, additional, Wang, Tianyun, additional, Hoekzema, Kendra, additional, Vives, Laura, additional, Vogel, Ida, additional, Brunner, Han G., additional, van der Burgt, Ineke, additional, Ockeloen, Charlotte W., additional, Schuurs-Hoeijmakers, Janneke H., additional, Klein Wassink-Ruiter, Jolien S., additional, Stumpel, Connie, additional, Stevens, Servi J.C., additional, Vles, Hans S., additional, Marcelis, Carlo M., additional, van Bokhoven, Hans, additional, Cantagrel, Vincent, additional, Colleaux, Laurence, additional, Nicouleau, Michael, additional, Lyonnet, Stanislas, additional, Bernier, Raphael A., additional, Gerdts, Jennifer, additional, Coe, Bradley P., additional, Romano, Corrado, additional, Alberti, Antonino, additional, Grillo, Lucia, additional, Scuderi, Carmela, additional, Nordenskjöld, Magnus, additional, Kvarnung, Malin, additional, Guo, Hui, additional, Xia, Kun, additional, Piton, Amélie, additional, Gerard, Bénédicte, additional, Genevieve, David, additional, Delobel, Bruno, additional, Lehalle, Daphne, additional, Perrin, Laurence, additional, Prieur, Fabienne, additional, Thevenon, Julien, additional, Gecz, Jozef, additional, Shaw, Marie, additional, Pfundt, Rolph, additional, Keren, Boris, additional, Jacquette, Aurelia, additional, Schenck, Annette, additional, Eichler, Evan E., additional, and Kleefstra, Tjitske, additional
Published: 2016
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36. Genotype–phenotype correlations in individuals with pathogenic <italic>RERE</italic> variants.

Author: Jordan, Valerie K., Fregeau, Brieana, Ge, Xiaoyan, Giordano, Jessica, Wapner, Ronald J., Balci, Tugce B., Carter, Melissa T., Bernat, John A., Moccia, Amanda N., Srivastava, Anshika, Martin, Donna M., Bielas, Stephanie L., Pappas, John, Svoboda, Melissa D., Rio, Marlène, Boddaert, Nathalie, Cantagrel, Vincent, Lewis, Andrea M., Scaglia, Fernando, and Undiagnosed Diseases Network
Abstract: Abstract: Heterozygous variants in the arginine‐glutamic acid dipeptide repeats gene (RERE) have been shown to cause neurodevelopmental disorder with or without anomalies of the brain, eye, or heart (NEDBEH). Here, we report nine individuals with NEDBEH who carry partial deletions or deleterious sequence variants in RERE. These variants were found to be de novo in all cases in which parental samples were available. An analysis of data from individuals with NEDBEH suggests that point mutations affecting the Atrophin‐1 domain of RERE are associated with an increased risk of structural eye defects, congenital heart defects, renal anomalies, and sensorineural hearing loss when compared with loss‐of‐function variants that are likely to lead to haploinsufficiency. A high percentage of RERE pathogenic variants affect a histidine‐rich region in the Atrophin‐1 domain. We have also identified a recurrent two‐amino‐acid duplication in this region that is associated with the development of a CHARGE syndrome‐like phenotype. We conclude that mutations affecting RERE result in a spectrum of clinical phenotypes. Genotype–phenotype correlations exist and can be used to guide medical decision making. Consideration should also be given to screening for RERE variants in individuals who fulfill diagnostic criteria for CHARGE syndrome but do not carry pathogenic variants in CHD7. [ABSTRACT FROM AUTHOR]
Published: 2018
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37. Recurrent KIF5C mutation leading to frontal pachygyria without microcephaly

Author: Cavallin, Mara, primary, Hubert, Laurence, additional, Cantagrel, Vincent, additional, Munnich, Arnold, additional, Boddaert, Nathalie, additional, Vincent-Delorme, Catherine, additional, Cuvellier, Jean Christophe, additional, Masson, Cecile, additional, Besmond, Claude, additional, and Bahi-Buisson, Nadia, additional
Published: 2015
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38. Identification of a novel ARL13B variant in a Joubert syndrome-affected patient with retinal impairment and obesity

Author: Thomas, Sophie, primary, Cantagrel, Vincent, additional, Mariani, Laura, additional, Serre, Valérie, additional, Lee, Ji-Eun, additional, Elkhartoufi, Nadia, additional, de Lonlay, Pascale, additional, Desguerre, Isabelle, additional, Munnich, Arnold, additional, Boddaert, Nathalie, additional, Lyonnet, Stanislas, additional, Vekemans, Michel, additional, Lisgo, Steven N, additional, Caspary, Tamara, additional, Gleeson, Joseph, additional, and Attié-Bitach, Tania, additional
Published: 2014
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39. AMPD2 Regulates GTP Synthesis and Is Mutated in a Potentially Treatable Neurodegenerative Brainstem Disorder

Author: Akizu, Naiara, primary, Cantagrel, Vincent, additional, Schroth, Jana, additional, Cai, Na, additional, Vaux, Keith, additional, McCloskey, Douglas, additional, Naviaux, Robert K., additional, Van Vleet, Jeremy, additional, Fenstermaker, Ali G., additional, Silhavy, Jennifer L., additional, Scheliga, Judith S., additional, Toyama, Keiko, additional, Morisaki, Hiroko, additional, Sonmez, Fatma M., additional, Celep, Figen, additional, Oraby, Azza, additional, Zaki, Maha S., additional, Al-Baradie, Raidah, additional, Faqeih, Eissa A., additional, Saleh, Mohammed A.M., additional, Spencer, Emily, additional, Rosti, Rasim Ozgur, additional, Scott, Eric, additional, Nickerson, Elizabeth, additional, Gabriel, Stacey, additional, Morisaki, Takayuki, additional, Holmes, Edward W., additional, and Gleeson, Joseph G., additional
Published: 2013
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40. Mutations in LAMB1 Cause Cobblestone Brain Malformation without Muscular or Ocular Abnormalities

Author: Radmanesh, Farid, primary, Caglayan, Ahmet Okay, additional, Silhavy, Jennifer L., additional, Yilmaz, Cahide, additional, Cantagrel, Vincent, additional, Omar, Tarek, additional, Rosti, Başak, additional, Kaymakcalan, Hande, additional, Gabriel, Stacey, additional, Li, Mingfeng, additional, Šestan, Nenad, additional, Bilguvar, Kaya, additional, Dobyns, William B., additional, Zaki, Maha S., additional, Gunel, Murat, additional, and Gleeson, Joseph G., additional
Published: 2013
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41. Mutations in the Glycosylphosphatidylinositol Gene PIGL Cause CHIME Syndrome

Author: Ng, Bobby G., primary, Hackmann, Karl, additional, Jones, Melanie A., additional, Eroshkin, Alexey M., additional, He, Ping, additional, Wiliams, Roy, additional, Bhide, Shruti, additional, Cantagrel, Vincent, additional, Gleeson, Joseph G., additional, Paller, Amy S., additional, Schnur, Rhonda E., additional, Tinschert, Sigrid, additional, Zunich, Janice, additional, Hegde, Madhuri R., additional, and Freeze, Hudson H., additional
Published: 2012
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42. Normal glycosylation screening does not rule out SRD5A3-CDG

Author: Mohamed, Miski, primary, Cantagrel, Vincent, additional, Al-Gazali, Lihadh, additional, Wevers, Ron A, additional, Lefeber, Dirk J, additional, and Morava, Eva, additional
Published: 2011
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43. Faulty Initiation of Proteoglycan Synthesis Causes Cardiac and Joint Defects

Author: Baasanjav, Sevjidmaa, primary, Al-Gazali, Lihadh, additional, Hashiguchi, Taishi, additional, Mizumoto, Shuji, additional, Fischer, Bjoern, additional, Horn, Denise, additional, Seelow, Dominik, additional, Ali, Bassam R., additional, Aziz, Samir A.A., additional, Langer, Ruth, additional, Saleh, Ahmed A.H., additional, Becker, Christian, additional, Nürnberg, Gudrun, additional, Cantagrel, Vincent, additional, Gleeson, Joseph G., additional, Gomez, Delphine, additional, Michel, Jean-Baptiste, additional, Stricker, Sigmar, additional, Lindner, Tom H., additional, Nürnberg, Peter, additional, Sugahara, Kazuyuki, additional, Mundlos, Stefan, additional, and Hoffmann, Katrin, additional
Published: 2011
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44. SRD5A3 Is Required for Converting Polyprenol to Dolichol and Is Mutated in a Congenital Glycosylation Disorder

Author: Cantagrel, Vincent, primary, Lefeber, Dirk J., additional, Ng, Bobby G., additional, Guan, Ziqiang, additional, Silhavy, Jennifer L., additional, Bielas, Stephanie L., additional, Lehle, Ludwig, additional, Hombauer, Hans, additional, Adamowicz, Maciej, additional, Swiezewska, Ewa, additional, De Brouwer, Arjan P., additional, Blümel, Peter, additional, Sykut-Cegielska, Jolanta, additional, Houliston, Scott, additional, Swistun, Dominika, additional, Ali, Bassam R., additional, Dobyns, William B., additional, Babovic-Vuksanovic, Dusica, additional, van Bokhoven, Hans, additional, Wevers, Ron A., additional, Raetz, Christian R.H., additional, Freeze, Hudson H., additional, Morava, Éva, additional, Al-Gazali, Lihadh, additional, and Gleeson, Joseph G., additional
Published: 2010
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45. Spatiotemporal expression in mouse brain of Kiaa2022, a gene disrupted in two patients with severe mental retardation

Author: Cantagrel, Vincent, primary, Haddad, Marie-Reine, additional, Ciofi, Philippe, additional, Andrieu, David, additional, Lossi, Anne-Marie, additional, Maldergem, Lionel van, additional, Roux, Jean-Christophe, additional, and Villard, Laurent, additional
Published: 2009
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46. Truncation ofNHEJ1 in a patient with polymicrogyria

Author: Cantagrel, Vincent, primary, Lossi, Anne-Marie, additional, Lisgo, Steven, additional, Missirian, Chantal, additional, Borges, Ana, additional, Philip, Nicole, additional, Fernandez, Carla, additional, Cardoso, Carlos, additional, Figarella-Branger, Dominique, additional, Moncla, Anne, additional, Lindsay, Susan, additional, Dobyns, William B., additional, and Villard, Laurent, additional
Published: 2007
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47. Identification of a novel ARL13B variant in a Joubert syndrome-affected patient with retinal impairment and obesity.

Author: Thomas, Sophie, Cantagrel, Vincent, Mariani, Laura, Serre, Valérie, Lee, Ji-Eun, Elkhartoufi, Nadia, de Lonlay, Pascale, Desguerre, Isabelle, Munnich, Arnold, Boddaert, Nathalie, Lyonnet, Stanislas, Vekemans, Michel, Lisgo, Steven N, Caspary, Tamara, Gleeson, Joseph, and Attié-Bitach, Tania
Subjects: *ADP-ribosylation factors, *JOUBERT syndrome, *RETINAL diseases, *OBESITY genetics, *GUANOSINE triphosphatase genetics, *CILIOPATHY, *GENETICS
Abstract: Joubert syndrome (JS) is a genetically heterogeneous autosomal recessive ciliopathy with 22 genes implicated to date, including a small, ciliary GTPase, ARL13B. ARL13B is required for cilia formation in vertebrates. JS patients display multiple symptoms characterized by ataxia due to the cerebellar vermis hypoplasia, and that can also include ocular abnormalities, renal cysts, liver fibrosis or polydactyly. These symptoms are shared with other ciliopathies, some of which display additional phenotypes, such as obesity. Here we identified a novel homozygous missense variant in ARL13B/JBTS8 in a JS patient who displayed retinal defects and obesity. We demonstrate the variant disrupts ARL13B function, as its expression did not rescue the mutant phenotype either in Arl13bscorpion zebrafish or in Arl13bhennin mouse embryonic fibroblasts, while the wild-type ARL13B did. Finally, we show that ARL13B is localized within the primary cilia of neonatal mouse hypothalamic neurons consistent with the known link between hypothalamic ciliary function and obesity. Thus our data identify a novel ARL13B variant that causes JS and retinopathy and suggest an extension of the phenotypic spectrum of ARL13B mutations to obesity. [ABSTRACT FROM AUTHOR]
Published: 2015
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48. Caractérisation par FISH, cartographie optique du génome et séquençage haut débit de génome de deux cas de triplication 16p13.11p11.2

Author: Nicolle, Romain, Siquier-Pernet, Karine, Rio, Marlène, Guimier, Anne, Olivier, Emmanuelle, Nitschke, Patrick, Bole-Feysot, Christine, Romana, Serge, Hastie, Alex, Cantagrel, Vincent, and Malan, Valérie
Abstract: Le bras court du chromosome 16 est caractérisé par l’existence de nombreuses duplications segmentaires prédisposant à des remaniements chromosomiques déséquilibrés par un mécanisme de recombinaison homologue non-allélique. Nous rapportons ici un nouveau désordre génomique du bras court du chromosome 16 diagnostiqué chez deux patientes non apparentées associant un retard du développement psychomoteur prédominant sur le langage et la marche, une hypotonie, une dysmorphie faciale ainsi qu’une surdité de transmission dans un contexte d’otites moyennes aiguës récurrentes. Les deux patientes sont porteuses d’une tétrasomie 16p13.11p11.2 d’une taille de 13 Mb survenue de novoet dont les points de cassure sont localisés dans des duplications segmentaires. La patiente 1 est également porteuse de la duplication récurrente 16p11.2 comprenant le gène SH2B1. Les études FISH ont montré que les 3 copies sur le chromosome 16 remanié sont disposées selon une orientation directe-inversée-directe. La position relative du locus du gène SH2B1 par rapport aux trois autres segments n’a pas pu être établie chez la patiente 1. Nous avons réalisé des analyses par cartographie optique du génome (Bionano Genomics) afin de mieux caractériser ces variants de structure chez ces deux patientes. L’analyse des fragments de jonction nous a permis de préciser l’organisation de la région remaniée et de proposer un mécanisme à l’origine de ces déséquilibres génomiques impliquant une recombinaison en U associée, dans un des cas, à une recombinaison homologue non-allélique. En raison de la localisation des points de cassure dans des duplications segmentaires, le séquençage haut débit de génome n’a pas permis de déterminer l’agencement des différents segments chromosomiques remaniés. Les nouvelles techniques de séquençage « long-reads » devraient être d’un grand apport dans ce type de situation.
Published: 2021
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49. Biallelic mutations in neurofascin cause neurodevelopmental impairment and peripheral demyelination

Author: Efthymiou, S., Salpietro, V., Malintan, N., Poncelet, M., Kriouile, Y., Fortuna, S., Zorzi, R. de, Payne, K., Henderson, L.B., Cortese, A., Maddirevula, S., Alhashmi, N., Wiethoff, S., Ryten, M., Botia, J.A., Provitera, V., Schuelke, M., Vandrovcova, J., Groppa, S., Karashova, B.M., Nachbauer, W., Boesch, S., Arning, L., Timmann, D., Cormand, B., Perez-Duenas, B., Goraya, J.S., Sultan, T., Mine, J., Avdjieva, D., Kathom, H., Tincheva, R., Banu, S., Pineda-Marfa, M., Veggiotti, P., Ferrari, M.D., Maagdenberg, A.M.J.M. van den, Verrotti, A., Marseglia, G., Savasta, S., Garcia-Silva, M., Ruiz, A.M., Garavaglia, B., Borgione, E., Portaro, S., Sanchez, B.M., Boles, R., Papacostas, S., Vikelis, M., Rothman, J., Kullmann, D., Papanicolaou, E.Z., Dardiotis, E., Maqbool, S., Ibrahim, S., Kirmani, S., Rana, N.N., Atawneh, O., Lim, S.Y., Shaikh, F., Koutsis, G., Breza, M., Mangano, S., Scuderi, C., Morello, G., Stojkovic, T., Zollo, M., Heimer, G., Dauvilliers, Y.A., Minetti, C., Al-Khawaja, I., Al-Mutairi, F., Hamed, S., Pipis, M., Bettencourt, C., Rinaldi, S., Walsh, L., Torti, E., Iodice, V., Najafi, M., Karimiani, E.G., Maroofian, R., Siquier-Pernet, K., Boddaert, N., Lonlay, P. de, Cantagrel, V., Aguennouz, M., Khorassani, M. el, Schmidts, M., Alkuraya, F.S., Edvardson, S., Nolano, M., Devaux, J., Houlden, H., SYNAPS Study Grp, Efthymiou, S., Salpietro, V., Malintan, N., Poncelet, M., Kriouile, Y., Fortuna, S., De Zorzi, R., Payne, K., Henderson, L. B., Cortese, A., Maddirevula, S., Alhashmi, N., Wiethoff, S., Ryten, M., Botia, J. A., Provitera, V., Schuelke, M., Vandrovcova, J., Walsh, L., Torti, E., Iodice, V., Najafi, M., Karimiani, E. G., Maroofian, R., Siquier-Pernet, K., Boddaert, N., De Lonlay, P., Cantagrel, V., Aguennouz, M., El Khorassani, M., Schmidts, M., Alkuraya, F. S., Edvardson, S., Nolano, M., Devaux, J., Houlden, H., Groppa, S., Karashova, B. M., Nachbauer, W., Boesch, S., Arning, L., Timmann, D., Cormand, B., Perez-Duenas, B., Goraya, J. S., Sultan, T., Mine, J., Avdjieva, D., Kathom, H., Tincheva, R., Banu, S., Pineda-Marfa, M., Veggiotti, P., Ferrari, M. D., Van Den Maagdenberg, A. M. J. M., Verrotti, A., Marseglia, G., Savasta, S., Garcia-Silva, M., Ruiz, A. M., Garavaglia, B., Borgione, E., Portaro, S., Sanchez, B. M., Boles, R., Papacostas, S., Vikelis, M., Rothman, J., Kullmann, D., Papanicolaou, E. Z., Dardiotis, E., Maqbool, S., Ibrahim, S., Kirmani, S., Rana, N. N., Atawneh, O., Lim, S. -Y., Shaikh, F., Koutsis, G., Breza, M., Mangano, S., Scuderi, C., Morello, G., Stojkovic, T., Zollo, M., Heimer, G., Dauvilliers, Y. A., Minetti, C., Al-Khawaja, I., Al-Mutairi, F., Hamed, S., Pipis, M., Bettencourt, C., Rinaldi, S., Institut des Neurosciences de Montpellier - Déficits sensoriels et moteurs (INM), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Montpellier (UM), Laboratory of Molecular Biophysics, Department of Biochemistry, Department of Biochemistry, Hertie Institute for Clinical Brain Research and Center for Neurology, University of Tübingen, Department of Medical and Molecular Genetics, King‘s College London, Department of Human Genetics, Ruhr University Bochum (RUB), Universitat de Barcelona (UB), Fondazione, Leiden University Medical Center (LUMC), Department of Physiology and Cellular Biophysics [New York, NY, USA], Columbia University College of Physicians and Surgeons, Department of Microbiology, Università degli studi di Catania [Catania], Institut de Myologie, Université Pierre et Marie Curie - Paris 6 (UPMC)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Association française contre les myopathies (AFM-Téléthon)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Ceinge, centro di Ingegneria Genetica e Biotecnologie Avanzate, Unité des troubles du sommeil, Centre de référence national sur les maladies rares (narcolepsie, hypersomnie idiopathique, syndrome de Kleine-Levin)-Hôpital Gui-de-Chauliac, Muscular and Neurodegenerative Disease Unit, University of Genoa (UNIGE), Department of Molecular Neuroscience, University College of London [London] (UCL)-Institute of Neurology, Indiana University, Indiana University [Bloomington], Indiana University System-Indiana University System, Molecular and Clinical Sciences Institute - St George’s [London, UK] (Genetics Research Centre), University of London [London], Imagine - Institut des maladies génétiques (IMAGINE - U1163), Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Neuroimagerie en psychiatrie (U1000), Université Paris-Sud - Paris 11 (UP11)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM), Service métabolisme, Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Université Paris Diderot - Paris 7 (UPD7)-CHU Necker - Enfants Malades [AP-HP], Department of Genetics and Metabolic Diseases and the Monique and Jacques Roboh Department of Genetic Research, Hadassah Hebrew University Medical Center [Jerusalem], Centre de recherche en neurobiologie - neurophysiologie de Marseille (CRN2M), Aix Marseille Université (AMU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Efthymiou S., Salpietro V., Malintan N., Poncelet M., Kriouile Y., Fortuna S., De Zorzi R., Payne K., Henderson L.B., Cortese A., Maddirevula S., Alhashmi N., Wiethoff S., Ryten M., Botia J.A., Provitera V., Schuelke M., Vandrovcova J., Walsh L., Torti E., Iodice V., Najafi M., Karimiani E.G., Maroofian R., Siquier-Pernet K., Boddaert N., De Lonlay P., Cantagrel V., Aguennouz M., El Khorassani M., Schmidts M., Alkuraya F.S., Edvardson S., Nolano M., Devaux J., Houlden H., Groppa S., Karashova B.M., Nachbauer W., Boesch S., Arning L., Timmann D., Cormand B., Perez-Duenas B., Goraya J.S., Sultan T., Mine J., Avdjieva D., Kathom H., Tincheva R., Banu S., Pineda-Marfa M., Veggiotti P., Ferrari M.D., Van Den Maagdenberg A.M.J.M., Verrotti A., Marseglia G., Savasta S., Garcia-Silva M., Ruiz A.M., Garavaglia B., Borgione E., Portaro S., Sanchez B.M., Boles R., Papacostas S., Vikelis M., Rothman J., Kullmann D., Papanicolaou E.Z., Dardiotis E., Maqbool S., Ibrahim S., Kirmani S., Rana N.N., Atawneh O., Lim S.-Y., Shaikh F., Koutsis G., Breza M., Mangano S., Scuderi C., Morello G., Stojkovic T., Zollo M., Heimer G., Dauvilliers Y.A., Minetti C., Al-Khawaja I., Al-Mutairi F., Hamed S., Pipis M., Bettencourt C., Rinaldi S., Efthymiou, Stephanie, Salpietro, Vincenzo, Malintan, Nancy, Poncelet, Mallory, Kriouile, Yamna, Fortuna, Sara, De Zorzi, Rita, Payne, Katelyn, Henderson, Lindsay B, Cortese, Andrea, Maddirevula, Sateesh, Alhashmi, Nadia, Wiethoff, Sarah, Ryten, Mina, Botia, Juan A, Provitera, Vincenzo, Schuelke, Marku, Vandrovcova, Jana, Walsh, Laurence, Torti, Erin, Iodice, Valeria, Najafi, Maryam, Karimiani, Ehsan Ghayoor, Maroofian, Reza, Siquier-Pernet, Karine, Boddaert, Nathalie, De Lonlay, Pascale, Cantagrel, Vincent, Aguennouz, Mhammed, El Khorassani, Mohamed, Schmidts, Miriam, Alkuraya, Fowzan S, Edvardson, Simon, Nolano, Maria, Devaux, Jérôme, Houlden, Henry, Université Pierre et Marie Curie - Paris 6 (UPMC)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Assistance publique - Hôpitaux de Paris (AP-HP) (APHP)-Association française contre les myopathies (AFM-Téléthon)-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)-Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM), Université Paris-Sud - Paris 11 (UP11)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Paris Descartes - Paris 5 (UPD5), Assistance publique - Hôpitaux de Paris (AP-HP) (APHP)-Université Paris Diderot - Paris 7 (UPD7)-CHU Necker - Enfants Malades [AP-HP], Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Association française contre les myopathies (AFM-Téléthon)-Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Pierre et Marie Curie - Paris 6 (UPMC), and Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Paris Descartes - Paris 5 (UPD5)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Sud - Paris 11 (UP11)
Subjects: Male, [SDV]Life Sciences [q-bio], [SDV.NEU.NB]Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]/Neurobiology, Nerve Fibers, Myelinated, Gene Frequency, Neurodevelopmental Disorder, [SDV.BC.IC]Life Sciences [q-bio]/Cellular Biology/Cell Behavior [q-bio.CB], Nerve Growth Factor, Protein Isoforms, Child, ComputingMilieux_MISCELLANEOUS, Myelin Sheath, neurofascin, neurodevelopment, peripheral demyelination, Allele, Demyelinating Disease, Genomics, neurodevelopment, neurofascin, peripheral demyelination, Settore MED/39 - Neuropsichiatria Infantile, Pedigree, [SDV.IMM.IA]Life Sciences [q-bio]/Immunology/Adaptive immunology, Child, Preschool, Peripheral Nerve, [SDV.NEU]Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC], Female, Neuroglia, Human, Adult, Adolescent, Nervous System Malformations, Guillain-Barre Syndrome, Axon, Nervous System Malformation, Ranvier's Nodes, Humans, Nerve Growth Factors, Peripheral Nerves, Alleles, Autoantibodies, Infant, Protein Isoform, Original Articles, Axons, nervous system, Neurodevelopmental Disorders, Cell Adhesion Molecule, Mutation, Cell Adhesion Molecules, Demyelinating Diseases
Abstract: See Karakaya and Wirth (doi:10.1093/brain/awz273) for a scientific commentary on this article. Neurofascin (NFASC) isoforms are immunoglobulin cell adhesion molecules involved in node of Ranvier assembly. Efthymiou et al. identify biallelic NFASC variants in ten unrelated patients with a neurodevelopmental disorder characterized by variable degrees of central and peripheral involvement. Abnormal expression of Nfasc155 is accompanied by severe loss of myelinated fibres., Axon pathfinding and synapse formation are essential processes for nervous system development and function. The assembly of myelinated fibres and nodes of Ranvier is mediated by a number of cell adhesion molecules of the immunoglobulin superfamily including neurofascin, encoded by the NFASC gene, and its alternative isoforms Nfasc186 and Nfasc140 (located in the axonal membrane at the node of Ranvier) and Nfasc155 (a glial component of the paranodal axoglial junction). We identified 10 individuals from six unrelated families, exhibiting a neurodevelopmental disorder characterized with a spectrum of central (intellectual disability, developmental delay, motor impairment, speech difficulties) and peripheral (early onset demyelinating neuropathy) neurological involvement, who were found by exome or genome sequencing to carry one frameshift and four different homozygous non-synonymous variants in NFASC. Expression studies using immunostaining-based techniques identified absent expression of the Nfasc155 isoform as a consequence of the frameshift variant and a significant reduction of expression was also observed in association with two non-synonymous variants affecting the fibronectin type III domain. Cell aggregation studies revealed a severely impaired Nfasc155-CNTN1/CASPR1 complex interaction as a result of the identified variants. Immunofluorescence staining of myelinated fibres from two affected individuals showed a severe loss of myelinated fibres and abnormalities in the paranodal junction morphology. Our results establish that recessive variants affecting the Nfasc155 isoform can affect the formation of paranodal axoglial junctions at the nodes of Ranvier. The genetic disease caused by biallelic NFASC variants includes neurodevelopmental impairment and a spectrum of central and peripheral demyelination as part of its core clinical phenotype. Our findings support possible overlapping molecular mechanisms of paranodal damage at peripheral nerves in both the immune-mediated and the genetic disease, but the observation of prominent central neurological involvement in NFASC biallelic variant carriers highlights the importance of this gene in human brain development and function.
Published: 2019

50. Biallelic mutations in SNX14 cause a syndromic form of cerebellar atrophy and lysosome-autophagosome dysfunction

Author: Keith K. Vaux, Mahmut Şamil Sağıroğlu, Laila Bastaki, Seth J. Field, Pascale de Lonlay, Sawsan Abdel-Hadi, Lihadh Al-Gazali, Hülya Kayserili, Ali Dursun, Jeffrey D. Esko, Eric Scott, Xin Wang, Faezeh Mojahedi, Ashleigh E. Schaffer, R. Köksal Özgül, Iman G. Mahmoud, Isabelle Desguerre, Matthew D. Buschman, Laila Selim, Samia A. Temtamy, Jean-Laurent Casanova, Murat Gunel, Abdelrahim Abdrabou Sadek, Philip L.S.M. Gordts, Brett Copeland, Mona Aglan, Amira Masri, Maha S. Zaki, Joseph G. Gleeson, Matloob Azam, Naiara Akizu, Vincent Cantagrel, Antoinette Gelot, Basak Rosti, Jennifer L. Silhavy, Esra Dikoglu, Ulrich Müller, Amera El Badawy, Gennaro Napolitano, Stacey Gabriel, Rasim Ozgur Rosti, Jana Schroth, Samira Ismail, Ghada M H Abdel-Salam, İç Hastalıkları, Akizu, Naiara, Cantagrel, Vincent, Zaki, Maha S., Al-Gazali, Lihadh, Wang, Xin, Rosti, Rasim Ozgur, Dikoglu, Esra, Gelot, Antoinette Bernabe, Rosti, Basak, Vaux, Keith K., Scott, Eric M., Silhavy, Jennifer L., Schroth, Jana, Copeland, Brett, Schaffer, Ashleigh E., Gordts, Philip L. S. M., Esko, Jeffrey D., Buschman, Matthew D., Field, Seth J., Napolitano, Gennaro, Abdel-Salam, Ghada M., Ozgul, R Koksal, Saglroglu, Mahmut Samil, Azam, Matloob, Ismail, Samira, Aglan, Mona, Selim, Laila, Mahmoud, Iman G., Abdel-Hadi, Sawsan, Badawy, Amera El, Sadek, Abdelrahim A., Mojahedi, Faezeh, Kayserili, Hulya, Masri, Amira, Bastaki, Laila, Temtamy, Samia, Müller, Ulrich, Desguerre, Isabelle, Casanova, Jean-Laurent, Dursun, Ali, Gunel, Murat, Gabriel, Stacey B., De Lonlay, Pascale, and Gleeson, Joseph G.
Subjects: Male, Autophagosome, medicine.disease_cause, Medical and Health Sciences, Lysosomal Storage Disease, Gene Frequency, Cerebellum, Phagosomes, Child, Sorting Nexins, Phagosome, Zebrafish, 2. Zero hunger, Genetics, Mutation, Cerebellar Disease, Syndrome, Biological Sciences, Lysosome, Cell biology, medicine.anatomical_structure, Child, Preschool, Female, Cerebellar atrophy, medicine.symptom, Human, Ataxia, Endosome, Biology, Article, Cerebellar Diseases, Clinical Research, Autophagy, medicine, Animals, Humans, Spinocerebellar Ataxias, Preschool, Spinocerebellar Ataxia, Animal, Sorting Nexin, Infant, Brain Disorders, Lysosomal Storage Diseases, Sorting nexin, Atrophy, Lod Score, Lysosomes, Developmental Biology
Abstract: Pediatric-onset ataxias often present clinically as developmental delay and intellectual disability, with prominent cerebellar atrophy as a key neuroradiographic finding. Here we describe a new clinically distinguishable recessive syndrome in 12 families with cerebellar atrophy together with ataxia, coarsened facial features and intellectual disability, due to truncating mutations in the sorting nexin gene SNX14, encoding a ubiquitously expressed modular PX domain-containing sorting factor. We found SNX14 localized to lysosomes and associated with phosphatidylinositol (3,5)-bisphosphate, a key component of late endosomes/lysosomes. Patient-derived cells showed engorged lysosomes and a slower autophagosome clearance rate upon autophagy induction by starvation. Zebrafish morphants for snx14 showed dramatic loss of cerebellar parenchyma, accumulation of autophagosomes and activation of apoptosis. Our results characterize a unique ataxia syndrome due to biallelic SNX14 mutations leading to lysosome-autophagosome dysfunction.
Published: 2015

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