Search

Your search keyword '"Anken, Eelco"' showing total 171 results
Start Over Author "Anken, Eelco" Publication Year Range Last 50 years
171 results on '"Anken, Eelco"'

3. A tetracationic porphyrin with dual anti-prion activity

Author

Masone, Antonio, Zucchelli, Chiara, Caruso, Enrico, Lavigna, Giada, Eraña, Hasier, Giachin, Gabriele, Tapella, Laura, Comerio, Liliana, Restelli, Elena, Raimondi, Ilaria, Elezgarai, Saioa R., De Leo, Federica, Quilici, Giacomo, Taiarol, Lorenzo, Oldrati, Marvin, Lorenzo, Nuria L., García-Martínez, Sandra, Cagnotto, Alfredo, Lucchetti, Jacopo, Gobbi, Marco, Vanni, Ilaria, Nonno, Romolo, Di Bari, Michele A., Tully, Mark D., Cecatiello, Valentina, Ciossani, Giuseppe, Pasqualato, Sebastiano, Van Anken, Eelco, Salmona, Mario, Castilla, Joaquín, Requena, Jesús R., Banfi, Stefano, Musco, Giovanna, and Chiesa, Roberto

Published
2023
Full Text
View/download PDF

6. Keratin 8 is a scaffolding and regulatory protein of ERAD complexes

Author

Pranke, Iwona Maria, Chevalier, Benoit, Premchandar, Aiswarya, Baatallah, Nesrine, Tomaszewski, Kamil F., Bitam, Sara, Tondelier, Danielle, Golec, Anita, Stolk, Jan, Lukacs, Gergely L., Hiemstra, Pieter S., Dadlez, Michal, Lomas, David A., Irving, James A., Delaunay-Moisan, Agnes, van Anken, Eelco, Hinzpeter, Alexandre, Sermet-Gaudelus, Isabelle, and Edelman, Aleksander

Published
2022
Full Text
View/download PDF

9. Messenger RNA targeting to endoplasmic reticulum stress signalling sites

Author

Aragón, Tomás, van Anken, Eelco, Pincus, David, Serafimova, Iana M, Korennykh, Alexei V, Rubio, Claudia A, and Walter, Peter

Subjects
Biochemistry and Cell Biology, Biological Sciences, Genetics, Biotechnology, Emerging Infectious Diseases, Underpinning research, 1.1 Normal biological development and functioning, Generic health relevance, 3' Untranslated Regions, Basic-Leucine Zipper Transcription Factors, Conserved Sequence, Endoplasmic Reticulum, Gene Expression Regulation, Fungal, Introns, Membrane Glycoproteins, Protein Biosynthesis, Protein Serine-Threonine Kinases, RNA Splicing, RNA, Fungal, RNA, Messenger, Repressor Proteins, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Signal Transduction, Stress, Physiological, General Science & Technology
Abstract

Deficiencies in the protein-folding capacity of the endoplasmic reticulum (ER) in all eukaryotic cells lead to ER stress and trigger the unfolded protein response (UPR). ER stress is sensed by Ire1, a transmembrane kinase/endoribonuclease, which initiates the non-conventional splicing of the messenger RNA encoding a key transcription activator, Hac1 in yeast or XBP1 in metazoans. In the absence of ER stress, ribosomes are stalled on unspliced HAC1 mRNA. The translational control is imposed by a base-pairing interaction between the HAC1 intron and the HAC1 5' untranslated region. After excision of the intron, transfer RNA ligase joins the severed exons, lifting the translational block and allowing synthesis of Hac1 from the spliced HAC1 mRNA to ensue. Hac1 in turn drives the UPR gene expression program comprising 7-8% of the yeast genome to counteract ER stress. Here we show that, on activation, Ire1 molecules cluster in the ER membrane into discrete foci of higher-order oligomers, to which unspliced HAC1 mRNA is recruited by means of a conserved bipartite targeting element contained in the 3' untranslated region. Disruption of either Ire1 clustering or HAC1 mRNA recruitment impairs UPR signalling. The HAC1 3' untranslated region element is sufficient to target other mRNAs to Ire1 foci, as long as their translation is repressed. Translational repression afforded by the intron fulfils this requirement for HAC1 mRNA. Recruitment of mRNA to signalling centres provides a new paradigm for the control of eukaryotic gene expression.

Published
2009

11. Time- and cost-effective production of untagged recombinant MVA by flow virometry and direct virus sorting.

Author

Daniela, Boselli, Panigada, Maddalena, Di Terlizzi, Simona, Romanò, Monica, Canonico, Emanuele, Villa, Chiara, Minici, Claudia, van Anken, Eelco, Soprana, Elisa, and Siccardi, Antonio G.

Subjects
GENE expression, CHIMERIC proteins, CELL fusion, WORKBENCHES, MOLECULAR cloning
Abstract

Background: Recombinant MVAs (rMVAs) are widely used both in basic and clinical research. Our previously developed Red-to-Green Gene Swapping Method (RGGSM), a cytometry-based Cell-Sorting protocol, revolves around the transient expression of a green fluorescent cytoplasmic marker, to subsequently obtain purified untagged rMVA upon loss of that marker by site-specific recombination. The standard RGSSM is quite costly in terms of bench work, reagents, and Sorting Facility fees. Although faster than other methods to obtain recombinant MVAs, the standard RGSSM still is time-consuming, taking at least 25 days to yield the final product. Methods: The direct sorting of fluorescent virions is made amenable by the marker HAG, a flu hemagglutinin/EGFP fusion protein, integrated into the external envelope of extracellular enveloped virions (EEVs). Fluorescent EEVs-containing supernatants of infected cultures are used instead of purified virus. Direct Virus-Sorting was performed on BD FACSAria Fusion cell sorter equipped with 4 lasers and a 100-mm nozzle, with 20 psi pressure and a minimal flow rate, validated using Megamix beads. Results: Upon infection of cells with recombinant EEVs, at the first sorting step virions that contain HAG are harvested and cloned, while the second sorting step yields EEVs that have lost HAG, allowing to clone untagged rMVA. Because only virion-containing supernatants are used, no virus purification steps and fewer sortings are necessary. Therefore, the final untagged rMVA product can be obtained in a mere 8 days. Conclusions: Altogether, we report that the original RGSSM has been markedly improved in terms of time- and cost efficiency by substituting Cell-Sorting with direct Virus-Sorting from the supernatants of infected cells. The improved virometry-based RGGSM may find wide applicability, considering that rMVAs hold great promise to serve as personalized vaccines for therapeutic intervention against cancer and various types of infectious diseases. [ABSTRACT FROM AUTHOR]

Published
2023
Full Text
View/download PDF

12. The importance of naturally attenuated SARS-CoV-2in the fight against COVID-19

Author

Armengaud, Jean [0000-0003-1589-445X], Thuret, Jean-Yves [0000-0001-5385-7620], Anken, Eelco van [0000-0001-9529-2701], Acosta-Alvear, Diego [0000-0002-1139-8486], Aragón, Tomás [0000-0002-1700-2729], Arias, Carolina [0000-0002-4445-0826], Blondel, Marc [0000-0003-4897-2995], Braakman, Ineke [0000-0003-1592-4364], Collet, Jean-François [0000-0001-8069-7036], Courcol, René [0000-0003-2324-5687], Danchin, Antoine [0000-0002-6350-5001], Deleuze, Jean-François [0000-0002-5358-4463], Lavigne, Jean-Philippe [0000-0002-9484-0304], Lucas, Sophie [0000-0003-1287-7996], Michiels, Thomas [0000-0001-9615-8053], Moore, Edward R.B. [0000-0001-7693-924X], Nixon-Abell, Jonathon [0000-0003-4169-0012], Rosselló-Mora, Ramón [0000-0001-8253-3107], Shi, Zheng-Li [0000-0001-8089-163X], Siccardi, Antonio G. [0000-0002-1654-5545], Sitia, Roberto [0000-0001-7086-4152], Tillett, Daniel [0000-0003-1061-0489], Timmis, Kenneth N. [0000-0002-0066-4670], Toledano, Michel B. [0000-0002-3079-1179], Sluijs, Peter van der [0000-0002-4485-3342], Vicenzi, Elisa [0000-0003-0051-3968], Armengaud, Jean, Delaunay, Agnes, Thuret, Jean-Yves, Anken, Eelco van, Acosta-Alvear, Diego, Aragón, Tomás, Arias, Carolina, Blondel, Marc, Braakman, Ineke, Collet, Jean-François, Courcol, René, Danchin, Antoine, Deleuze, Jean-François, Lavigne, Jean-Philippe, Lucas, Sophie, Michiels, Thomas, Moore, Edward R.B., Nixon-Abell, Jonathon, Rosselló-Mora, Ramón, Shi, Zheng-Li, Siccardi, Antonio G., Sitia, Roberto, Tillett, Daniel, Timmis, Kenneth N., Toledano, Michel B., Sluijs, Peter van der, Vicenzi, Elisa, Armengaud, Jean [0000-0003-1589-445X], Thuret, Jean-Yves [0000-0001-5385-7620], Anken, Eelco van [0000-0001-9529-2701], Acosta-Alvear, Diego [0000-0002-1139-8486], Aragón, Tomás [0000-0002-1700-2729], Arias, Carolina [0000-0002-4445-0826], Blondel, Marc [0000-0003-4897-2995], Braakman, Ineke [0000-0003-1592-4364], Collet, Jean-François [0000-0001-8069-7036], Courcol, René [0000-0003-2324-5687], Danchin, Antoine [0000-0002-6350-5001], Deleuze, Jean-François [0000-0002-5358-4463], Lavigne, Jean-Philippe [0000-0002-9484-0304], Lucas, Sophie [0000-0003-1287-7996], Michiels, Thomas [0000-0001-9615-8053], Moore, Edward R.B. [0000-0001-7693-924X], Nixon-Abell, Jonathon [0000-0003-4169-0012], Rosselló-Mora, Ramón [0000-0001-8253-3107], Shi, Zheng-Li [0000-0001-8089-163X], Siccardi, Antonio G. [0000-0002-1654-5545], Sitia, Roberto [0000-0001-7086-4152], Tillett, Daniel [0000-0003-1061-0489], Timmis, Kenneth N. [0000-0002-0066-4670], Toledano, Michel B. [0000-0002-3079-1179], Sluijs, Peter van der [0000-0002-4485-3342], Vicenzi, Elisa [0000-0003-0051-3968], Armengaud, Jean, Delaunay, Agnes, Thuret, Jean-Yves, Anken, Eelco van, Acosta-Alvear, Diego, Aragón, Tomás, Arias, Carolina, Blondel, Marc, Braakman, Ineke, Collet, Jean-François, Courcol, René, Danchin, Antoine, Deleuze, Jean-François, Lavigne, Jean-Philippe, Lucas, Sophie, Michiels, Thomas, Moore, Edward R.B., Nixon-Abell, Jonathon, Rosselló-Mora, Ramón, Shi, Zheng-Li, Siccardi, Antonio G., Sitia, Roberto, Tillett, Daniel, Timmis, Kenneth N., Toledano, Michel B., Sluijs, Peter van der, and Vicenzi, Elisa

Abstract

The current SARS‐CoV‐2 pandemic is wreaking havoc throughout the world and has rapidly become a global health emergency. A central question concerning COVID‐19 is why some individuals become sick and others not. Many have pointed already at variation in risk factors between individuals. However, the variable outcome of SARS‐CoV‐2 infections may, at least in part, be due also to differences between the viral subspecies with which individuals are infected. A more pertinent question is how we are to overcome the current pandemic. A vaccine against SARS‐CoV‐2 would offer significant relief, although vaccine developers have warned that design, testing and production of vaccines may take a year if not longer. Vaccines are based on a handful of different designs (i), but the earliest vaccines were based on the live, attenuated virus. As has been the case for other viruses during earlier pandemics, SARS‐CoV‐2 will mutate and may naturally attenuate over time (ii). What makes the current pandemic unique is that, thanks to state‐of‐the‐art nucleic acid sequencing technologies, we can follow in detail how SARS‐CoV‐2 evolves while it spreads. We argue that knowledge of naturally emerging attenuated SARS‐CoV‐2 variants across the globe should be of key interest in our fight against the pandemic.

Published
2020

13. The importance of naturally attenuated SARS‐CoV ‐2 in the fight against COVID ‐19

Author

Armengaud, Jean, Delaunay‐Moisan, Agnès, Thuret, Jean‐Yves, Anken, Eelco, Acosta‐Alvear, Diego, Aragón, Tomás, Arias, Carolina, Blondel, Marc, Braakman, Ineke, Collet, Jean‐François, Courcol, René, Danchin, Antoine, Deleuze, Jean‐François, Lavigne, Jean‐Philippe, Lucas, Sophie, Michiels, Thomas, Moore, Edward R. B., Nixon‐Abell, Jonathon, Rossello‐Mora, Ramon, Shi, Zheng‐Li, Siccardi, Antonio G., Sitia, Roberto, Tillett, Daniel, Timmis, Kenneth N., Toledano, Michel B., Sluijs, Peter, Vicenzi, Elisa, Médicaments et Technologies pour la Santé (MTS), Université Paris-Saclay-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), 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), Stress Oxydatif et Cancer (SOC), Département Biologie Cellulaire (BioCell), 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 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)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS), Sénescence et stabilité génomique (SEN), Département Biologie des Génomes (DBG), San Raffaele Scientific Institute, Vita-Salute San Raffaele University and Center for Translational Genomics and Bioinformatics, University of California [Santa Barbara] (UC Santa Barbara), University of California (UC), Universidad Pública de Navarra [Espagne] = Public University of Navarra (UPNA), Génétique, génomique fonctionnelle et biotechnologies (UMR 1078) (GGB), EFS-Université de Brest (UBO)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Institut Brestois Santé Agro Matière (IBSAM), Université de Brest (UBO), Université de Bretagne Occidentale - UFR Médecine et Sciences de la Santé (UBO UFR MSS), Utrecht University [Utrecht], Université Catholique de Louvain = Catholic University of Louvain (UCL), Walloon Excellence in Life sciences and BIOtechnology [Liège] (WELBIO), 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 Paris Cité (UPCité), Centre National de Recherche en Génomique Humaine (CNRGH), Commissariat à l'énergie atomique et aux énergies alternatives (CEA), Institut de Biologie François JACOB (JACOB), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA), Virulence bactérienne et maladies infectieuses (VBMI), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Montpellier (UM), University of Gothenburg (GU), Sahlgrenska University Hospital [Gothenburg], University of Cambridge [UK] (CAM), Institut Mediterrani d'Estudis Avancats (IMEDEA), Consejo Superior de Investigaciones Científicas [Madrid] (CSIC)-Universidad de las Islas Baleares (UIB), Wuhan Institute of Virology [Wuhan, China], Chinese Academy of Sciences [Wuhan Branch], Technische Universität Braunschweig = Technical University of Braunschweig [Braunschweig], ANR-17-CE18-0023,Phylopeptidomics,Identification rapide de bactéries pathogènes et résistances aux antibiotiques(2017), Armengaud, Jean [0000-0003-1589-445X], Thuret, Jean-Yves [0000-0001-5385-7620], Anken, Eelco van [0000-0001-9529-2701], Acosta-Alvear, Diego [0000-0002-1139-8486], Aragón, Tomás [0000-0002-1700-2729], Arias, Carolina [0000-0002-4445-0826], Blondel, Marc [0000-0003-4897-2995], Braakman, Ineke [0000-0003-1592-4364], Collet, Jean-François [0000-0001-8069-7036], Courcol, René [0000-0003-2324-5687], Danchin, Antoine [0000-0002-6350-5001], Deleuze, Jean-François [0000-0002-5358-4463], Lavigne, Jean-Philippe [0000-0002-9484-0304], Lucas, Sophie [0000-0003-1287-7996], Michiels, Thomas [0000-0001-9615-8053], Moore, Edward R.B. [0000-0001-7693-924X], Nixon-Abell, Jonathon [0000-0003-4169-0012], Rosselló-Mora, Ramón [0000-0001-8253-3107], Shi, Zheng-Li [0000-0001-8089-163X], Siccardi, Antonio G. [0000-0002-1654-5545], Sitia, Roberto [0000-0001-7086-4152], Tillett, Daniel [0000-0003-1061-0489], Timmis, Kenneth N. [0000-0002-0066-4670], Toledano, Michel B. [0000-0002-3079-1179], Sluijs, Peter van der [0000-0002-4485-3342], Vicenzi, Elisa [0000-0003-0051-3968], University of California [Santa Barbara] (UCSB), University of California, Institut Brestois Santé Agro Matière (IBSAM), Université de Brest (UBO)-Université de Brest (UBO)-EFS-Institut National de la Santé et de la Recherche Médicale (INSERM), Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université de Paris (UP), Technical University Braunschweig, Armengaud, Jean, Thuret, Jean-Yves, Anken, Eelco van, Acosta-Alvear, Diego, Aragón, Tomás, Arias, Carolina, Blondel, Marc, Braakman, Ineke, Collet, Jean-François, Courcol, René, Danchin, Antoine, Deleuze, Jean-François, Lavigne, Jean-Philippe, Lucas, Sophie, Michiels, Thomas, Moore, Edward R.B., Nixon-Abell, Jonathon, Rosselló-Mora, Ramón, Shi, Zheng-Li, Siccardi, Antonio G., Sitia, Roberto, Tillett, Daniel, Timmis, Kenneth N., Toledano, Michel B., Sluijs, Peter van der, Vicenzi, Elisa, Armengaud, J., Delaunay-Moisan, A., Thuret, J. -Y., van Anken, E., Acosta-Alvear, D., Aragon, T., Arias, C., Blondel, M., Braakman, I., Collet, J. -F., Courcol, R., Danchin, A., Deleuze, J. -F., Lavigne, J. -P., Lucas, S., Michiels, T., Moore, E. R. B., Nixon-Abell, J., Rossello-Mora, R., Shi, Z., Siccardi, A. G., Sitia, R., Tillett, D., Timmis, K. N., Toledano, M. B., van der Sluijs, P., Vicenzi, E., and UCL - SSS/DDUV - Institut de Duve

Subjects
Opinion, viruses, Pneumonia, Viral, Gene Expression, Microbiology, Disease Outbreaks, Evolution, Molecular, Betacoronavirus, [SDV.MHEP.MI]Life Sciences [q-bio]/Human health and pathology/Infectious diseases, Animals, Humans, Health emergency, Selection, Genetic, Pandemics, Ecology, Evolution, Behavior and Systematics, [SDV.MHEP.ME]Life Sciences [q-bio]/Human health and pathology/Emerging diseases, Virulence, SARS-CoV-2, fungi, COVID-19, SARS Virus, Adaptation, Physiological, Severe acute respiratory syndrome-related coronavirus, Host-Pathogen Interactions, Mutation, Spike Glycoprotein, Coronavirus, [SDV.MP.VIR]Life Sciences [q-bio]/Microbiology and Parasitology/Virology, Coronavirus Infections
Abstract

The current SARS‐CoV‐2 pandemic is wreaking havoc throughout the world and has rapidly become a global health emergency. A central question concerning COVID‐19 is why some individuals become sick and others not. Many have pointed already at variation in risk factors between individuals. However, the variable outcome of SARS‐CoV‐2 infections may, at least in part, be due also to differences between the viral subspecies with which individuals are infected. A more pertinent question is how we are to overcome the current pandemic. A vaccine against SARS‐CoV‐2 would offer significant relief, although vaccine developers have warned that design, testing and production of vaccines may take a year if not longer. Vaccines are based on a handful of different designs (i), but the earliest vaccines were based on the live, attenuated virus. As has been the case for other viruses during earlier pandemics, SARS‐CoV‐2 will mutate and may naturally attenuate over time (ii). What makes the current pandemic unique is that, thanks to state‐of‐the‐art nucleic acid sequencing technologies, we can follow in detail how SARS‐CoV‐2 evolves while it spreads. We argue that knowledge of naturally emerging attenuated SARS‐CoV‐2 variants across the globe should be of key interest in our fight against the pandemic.

Published
2020
Full Text
View/download PDF

14. Keratin 8 is a scaffolding and regulatory protein of ERAD complexes

Author

Pranke, Iwona M., primary, Chevalier, Benoit, additional, Premchandar, Aiswarya, additional, Baatallah, Nesrine, additional, Tomaszewski, Kamil F., additional, Bitam, Sara, additional, Tondelier, Danielle, additional, Golec, Anita, additional, Stolk, Jan, additional, Lukacs, Gergely L., additional, Hiemstra, Pieter S., additional, Dadlez, Michal, additional, Lomas, David A., additional, Irving, James A., additional, Delaunay-Moisan, Agnes, additional, van Anken, Eelco, additional, Hinzpeter, Alexandre, additional, Sermet-Gaudelus, Isabelle, additional, and Edelman, Aleksander, additional

Published
2022
Full Text
View/download PDF

16. Cutting Edge: IgE Plays an Active Role in Tumor Immunosurveillance in Mice

Author

Nigro, Elisa A., Brini, Anna T., Yenagi, Vijay A., Ferreira, Lorena M., Achatz Straussberger, Gertrude, Sanvito, Francesca, Soprana, Elisa, Van Anken, Eelco, Achatz, Gernot, Siccardi, Antonio G., Vangelista, Luca, VAN ANKEN, EELCO, AMBROSI, ALESSANDRO, Nigro, Elisa A., Brini, Anna T., Yenagi, Vijay A., Ferreira, Lorena M., Achatz Straussberger, Gertrude, Ambrosi, Alessandro, Sanvito, Francesca, Soprana, Elisa, Van Anken, Eelco, Achatz, Gernot, Siccardi, Antonio G., Vangelista, Luca, and VAN ANKEN, Eelco

Subjects
0301 basic medicine, medicine.medical_treatment, Immunology, Immunoglobulin E, Atopy, Mice, 03 medical and health sciences, 0302 clinical medicine, Adjuvants, Immunologic, IgE deficiency, Neoplasms, medicine, Animals, Immunology and Allergy, Receptor, Immunologic Surveillance, Mice, Knockout, Mice, Inbred BALB C, biology, Receptors, IgE, Cancer, Immunotherapy, medicine.disease, 030104 developmental biology, biology.protein, Genetic Engineering, Adjuvant, CD8, 030215 immunology
Abstract

Exogenous IgE acts as an adjuvant in tumor vaccination in mice, and therefore a direct role of endogenous IgE in tumor immunosurveillance was investigated. By using genetically engineered mice, we found that IgE ablation rendered mice more susceptible to the growth of transplantable tumors. Conversely, a strengthened IgE response provided mice with partial or complete resistance to tumor growth, depending on the tumor type. By genetic crosses, we showed that IgE-mediated tumor protection was mostly lost in mice lacking FcεRI. Tumor protection was also lost after depletion of CD8+ T cells, highlighting a cross-talk between IgE and T cell–mediated tumor immunosurveillance. Our findings provide the rationale for clinical observations that relate atopy with a lower risk for developing cancer and open new avenues for the design of immunotherapeutics relevant for clinical oncology.

Published
2016

19. Efficient IgM assembly and secretion require the plasma cell induced endoplasmic reticulum protein pERp1

Author

van Anken, Eelco, Pena, Florentina, Hafkemeijer, Nicole, Christis, Chantal, Romijn, Edwin P., Oorschot, Ulla Grauschop Viola M.J., Pertel, Thomas, Engels, Sander, Ora, Ari, Lastun, Viorica, Glockshuber, Rudi, Klumperman, Judith, Heck, Albert J.R., Luban, Jeremy, and Braakman, Ineke

Subjects
Immunoglobulins -- Research, Endoplasmic reticulum -- Research, Protein folding -- Research, Science and technology
Abstract

Plasma cells daily secrete their own mass in antibodies, which fold and assemble in the endoplasmic reticulum (ER). To reach these levels, cells require pERp1, a novel lymphocyte-specific small ER-resident protein, which attains expression levels as high as BiP when B cells differentiate into plasma cells. Although pERp1 has no homology with known ER proteins, it does contain a CXXC motif typical for oxidoreductases. In steady state, the CXXC cysteines are locked by two parallel disulfide bonds with a downstream C[(X).sub.6]C motif, and pERp1 displays only modest oxidoreductase activity, pERpl emerged as a dedicated folding factor for IgM, associating with both heavy and light chains and promoting assembly and secretion of mature IgM.

Published
2009

20. The B-cell receptor controls fitness of MYC-driven lymphoma cells via GSK3 inhibition

Author

Varano, Gabriele, Raffel, Simon, Sormani, Martina, Zanardi, Federica, Lonardi, Silvia, Zasada, Christin, Perucho, Laura, Petrocelli, Valentina, Haake, Andrea, Lee, Albert K., Bugatti, Mattia, Paul, Ulrike, Van Anken, Eelco, Pasqualucci, Laura, Rabadan, Raul, Siebert, Reiner, Kempa, Stefan, Ponzoni, Maurilio, Facchetti, Fabio, Rajewsky, Klaus, and Casola, Stefano

Subjects
B cells -- Health aspects, Lymphomas -- Genetic aspects, Transcription factors -- Health aspects, Environmental issues, Science and technology, Zoology and wildlife conservation
Abstract

Author(s): Gabriele Varano [1]; Simon Raffel [2]; Martina Sormani [1]; Federica Zanardi [1]; Silvia Lonardi [3]; Christin Zasada [4]; Laura Perucho [1]; Valentina Petrocelli [1]; Andrea Haake [5]; Albert K. [...]

Published
2017
Full Text
View/download PDF

21. The importance of naturally attenuated SARS‐CoV‐2in the fight against COVID‐19

Author

Armengaud, Jean, primary, Delaunay‐Moisan, Agnès, additional, Thuret, Jean‐Yves, additional, van Anken, Eelco, additional, Acosta‐Alvear, Diego, additional, Aragón, Tomás, additional, Arias, Carolina, additional, Blondel, Marc, additional, Braakman, Ineke, additional, Collet, Jean‐François, additional, Courcol, René, additional, Danchin, Antoine, additional, Deleuze, Jean‐François, additional, Lavigne, Jean‐Philippe, additional, Lucas, Sophie, additional, Michiels, Thomas, additional, Moore, Edward R. B., additional, Nixon‐Abell, Jonathon, additional, Rossello‐Mora, Ramon, additional, Shi, Zheng‐Li, additional, Siccardi, Antonio G., additional, Sitia, Roberto, additional, Tillett, Daniel, additional, Timmis, Kenneth N., additional, Toledano, Michel B., additional, van der Sluijs, Peter, additional, and Vicenzi, Elisa, additional

Published
2020
Full Text
View/download PDF

24. A selective ER‐phagy exerts procollagen quality control via a Calnexin‐FAM134B complex

Author

Forrester, Alison, Leonibus, Chiara De, Grumati, Paolo, Fasana, Elisa, Piemontese, Marilina, Staiano, Leopoldo, Fregno, Ilaria, Raimondi, Andrea, Marazza, Alessandro, Bruno, Gemma, Iavazzo, Maria, Intartaglia, Daniela, Seczynska, Marta, van Anken, Eelco, Conte, Ivan, De Matteis, Maria Antonietta, Dikic, Ivan, Molinari, Maurizio, Settembre, Carmine, Forrester, Alison, Leonibus, Chiara De, Grumati, Paolo, Fasana, Elisa, Piemontese, Marilina, Staiano, Leopoldo, Fregno, Ilaria, Raimondi, Andrea, Marazza, Alessandro, Bruno, Gemma, Iavazzo, Maria, Intartaglia, Daniela, Seczynska, Marta, van Anken, Eelco, Conte, Ivan, De Matteis, Maria Antonietta, Dikic, Ivan, Molinari, Maurizio, and Settembre, Carmine

Abstract

Autophagy is a cytosolic quality control process that recognizes substrates through receptor‐mediated mechanisms. Procollagens, the most abundant gene products in Metazoa, are synthesized in the endoplasmic reticulum (ER), and a fraction that fails to attain the native structure is cleared by autophagy. However, how autophagy selectively recognizes misfolded procollagens in the ER lumen is still unknown. We performed siRNA interference, CRISPR‐Cas9 or knockout‐mediated gene deletion of candidate autophagy and ER proteins in collagen producing cells. We found that the ER‐resident lectin chaperone Calnexin (CANX) and the ER‐phagy receptor FAM134B are required for autophagy‐mediated quality control of endogenous procollagens. Mechanistically, CANX acts as co‐receptor that recognizes ER luminal misfolded procollagens and interacts with the ER‐phagy receptor FAM134B. In turn, FAM134B binds the autophagosome membrane‐associated protein LC3 and delivers a portion of ER containing both CANX and procollagen to the lysosome for degradation. Thus, a crosstalk between the ER quality control machinery and the autophagy pathway selectively disposes of proteasome‐resistant misfolded clients from the ER.

Published
2019

30. Inadequate BiP availability defines endoplasmic reticulum stress

Author

Vitale, Milena, primary, Bakunts, Anush, additional, Orsi, Andrea, additional, Lari, Federica, additional, Tadè, Laura, additional, Danieli, Alberto, additional, Rato, Claudia, additional, Valetti, Caterina, additional, Sitia, Roberto, additional, Raimondi, Andrea, additional, Christianson, John C, additional, and van Anken, Eelco, additional

Published
2019
Full Text
View/download PDF

32. A selective ER ‐phagy exerts procollagen quality control via a Calnexin‐ FAM 134B complex

Author

Forrester, Alison, primary, De Leonibus, Chiara, additional, Grumati, Paolo, additional, Fasana, Elisa, additional, Piemontese, Marilina, additional, Staiano, Leopoldo, additional, Fregno, Ilaria, additional, Raimondi, Andrea, additional, Marazza, Alessandro, additional, Bruno, Gemma, additional, Iavazzo, Maria, additional, Intartaglia, Daniela, additional, Seczynska, Marta, additional, Anken, Eelco, additional, Conte, Ivan, additional, De Matteis, Maria Antonietta, additional, Dikic, Ivan, additional, Molinari, Maurizio, additional, and Settembre, Carmine, additional

Published
2018
Full Text
View/download PDF

33. A pH-Regulated Quality Control Cycle for Surveillance of Secretory Protein Assembly

Author

Vavassori, S, Cortini, M, Masui, S, Sannino, S, Anelli, T, Caserta, IR, Fagioli, C, Mossuto, MF, Fornili, A, van Anken, E, Degano, M, Inaba, K, VAN ANKEN, EELCO, SITIA , ROBERTO, Vavassori, S, Cortini, M, Masui, S, Sannino, S, Anelli, T, Caserta, Ir, Fagioli, C, Mossuto, Mf, Fornili, A, van Anken, E, Degano, M, Inaba, K, Sitia, Roberto, and VAN ANKEN, Eelco

Subjects
PROTEIN SECRETION, Models, Molecular, PROTEOSTASIS, Amino Acid Motifs, Golgi Apparatus, Biology, Endoplasmic Reticulum, Article, Calnexin, Catalytic Domain, Humans, Secretion, ERp44, Binding site, Molecular Biology, Secretory pathway, Membrane Glycoproteins, Secretory Pathway, Endoplasmic reticulum, Cell Cycle, Membrane Proteins, Cell Biology, Hydrogen-Ion Concentration, Cell biology, Transport protein, Protein Transport, Secretory protein, Amino Acid Substitution, biology.protein, Mutagenesis, Site-Directed, Protein Multimerization, Oxidoreductases, Calreticulin, HeLa Cells, Molecular Chaperones
Abstract

Summary To warrant the quality of the secretory proteome, stringent control systems operate at the endoplasmic reticulum (ER)-Golgi interface, preventing the release of nonnative products. Incompletely assembled oligomeric proteins that are deemed correctly folded must rely on additional quality control mechanisms dedicated to proper assembly. Here we unveil how ERp44 cycles between cisGolgi and ER in a pH-regulated manner, patrolling assembly of disulfide-linked oligomers such as IgM and adiponectin. At neutral, ER-equivalent pH, the ERp44 carboxy-terminal tail occludes the substrate-binding site. At the lower pH of the cisGolgi, conformational rearrangements of this peptide, likely involving protonation of ERp44’s active cysteine, simultaneously unmask the substrate binding site and −RDEL motif, allowing capture of orphan secretory protein subunits and ER retrieval via KDEL receptors. The ERp44 assembly control cycle couples secretion fidelity and efficiency downstream of the calnexin/calreticulin and BiP-dependent quality control cycles., Graphical Abstract, Highlights • ERp44 governs a pH-regulated assembly control cycle in the early secretory pathway • Accessibility of ERp44’s active site and –RDEL ER retrieval motif is pH dependent • Unmasking of ERp44’s active site likely involves protonation of cysteine 29 • ERp44 captures client proteins at cisGolgi-equivalent pH for retrieval to the ER

Published
2013

34. The carbohydrate at asparagine 386 on HIV-1 gp120 is not essential for protein folding and function but is involved in immune evasion

Author

Groot Fedde, Dankers Martijn M, Busser Els, Melchers Mark, Eggink Dirk, Bontjer Ilja, Liscaljet I Marije, Nabatov Alexei A, van Anken Eelco, Sanders Rogier W, Braakman Ineke, Berkhout Ben, and Paxton William A

Subjects
Immunologic diseases. Allergy, RC581-607
Abstract

Abstract Background The HIV-1 envelope glycoprotein gp120, which mediates viral attachment to target cells, consists for ~50% of sugar, but the role of the individual sugar chains in various aspects of gp120 folding and function is poorly understood. Here we studied the role of the carbohydrate at position 386. We identified a virus variant that had lost the 386 glycan in an evolution study of a mutant virus lacking the disulfide bond at the base of the V4 domain. Results The 386 carbohydrate was not essential for folding of wt gp120. However, its removal improved folding of a gp120 variant lacking the 385–418 disulfide bond, suggesting that it plays an auxiliary role in protein folding in the presence of this disulfide bond. The 386 carbohydrate was not critical for gp120 binding to dendritic cells (DC) and DC-mediated HIV-1 transmission to T cells. In accordance with previous reports, we found that N386 was involved in binding of the mannose-dependent neutralizing antibody 2G12. Interestingly, in the presence of specific substitutions elsewhere in gp120, removal of N386 did not result in abrogation of 2G12 binding, implying that the contribution of N386 is context dependent. Neutralization by soluble CD4 and the neutralizing CD4 binding site (CD4BS) antibody b12 was significantly enhanced in the absence of the 386 sugar, indicating that this glycan protects the CD4BS against antibodies. Conclusion The carbohydrate at position 386 is not essential for protein folding and function, but is involved in the protection of the CD4BS from antibodies. Removal of this sugar in the context of trimeric Env immunogens may therefore improve the elicitation of neutralizing CD4BS antibodies.

Published
2008
Full Text
View/download PDF

35. A selective ER‐phagy exerts procollagen quality control via a Calnexin‐FAM134B complex

Author

Forrester, Alison, De Leonibus, Chiara, Grumati, Paolo, Fasana, Elisa, Piemontese, Marilina, Staiano, Leopoldo, Fregno, Ilaria, Raimondi, Andrea, Marazza, Alessandro, Bruno, Gemma, Iavazzo, Maria, Intartaglia, Daniela, Seczynska, Marta, Anken, Eelco van, Conte, Ivan, De Matteis, Maria Antonietta, Đikić, Ivan, Molinari, Maurizio, Settembre, Carmine, Forrester, Alison, De Leonibus, Chiara, Grumati, Paolo, Fasana, Elisa, Piemontese, Marilina, Staiano, Leopoldo, Fregno, Ilaria, Raimondi, Andrea, Marazza, Alessandro, Bruno, Gemma, Iavazzo, Maria, Intartaglia, Daniela, Seczynska, Marta, Anken, Eelco van, Conte, Ivan, De Matteis, Maria Antonietta, Đikić, Ivan, Molinari, Maurizio, and Settembre, Carmine

Abstract

Autophagy is a cytosolic quality control process that recognizes substrates through receptor‐mediated mechanisms. Procollagens, the most abundant gene products in Metazoa, are synthesized in the endoplasmic reticulum (ER), and a fraction that fails to attain the native structure is cleared by autophagy. However, how autophagy selectively recognizes misfolded procollagens in the ER lumen is still unknown. We performed siRNA interference, CRISPR‐Cas9 or knockout‐mediated gene deletion of candidate autophagy and ER proteins in collagen producing cells. We found that the ER‐resident lectin chaperone Calnexin (CANX) and the ER‐phagy receptor FAM134B are required for autophagy‐mediated quality control of endogenous procollagens. Mechanistically, CANX acts as co‐receptor that recognizes ER luminal misfolded procollagens and interacts with the ER‐phagy receptor FAM134B. In turn, FAM134B binds the autophagosome membrane‐associated protein LC3 and delivers a portion of ER containing both CANX and procollagen to the lysosome for degradation. Thus, a crosstalk between the ER quality control machinery and the autophagy pathway selectively disposes of proteasome‐resistant misfolded clients from the ER.

Published
2018

36. No evidence for cell‐to‐cell transmission of the unfolded protein response in cell culture.

Author

Ziel, Anna M., Wolzak, Kimberly, Nölle, Anna, Hoetjes, Petrus J., Berenjeno‐Correa, Ernesto, Anken, Eelco, Struys, Eduard A., and Scheper, Wiep

Subjects
CELL culture, IMMUNOGLOBULIN heavy chains, HELA cells, NEURODEGENERATION, PROTEIN expression, IMMUNOGLOBULIN M
Abstract

The unfolded protein response (UPR) is one of the major cell‐autonomous proteostatic stress responses. The UPR has been implicated in the pathogenesis of neurodegenerative diseases and is therefore actively investigated as therapeutic target. In this respect, cell non‐autonomous effects of the UPR including the reported cell‐to‐cell transmission of UPR activity may be highly important. A pharmaca‐based UPR induction was employed to generate conditioned media (CM) from CM‐donating neuronal ('donor') cells (SK‐N‐SH and primary mouse neurons). As previously reported, upon subsequent transfer of CM to naive neuronal 'acceptor' cells, we confirmed UPR target mRNA and protein expression by qPCR and automated microscopy. However, UPR target gene expression was also induced in the absence of donor cells, indicating carry‐over of pharmaca. Genetic induction of single pathways of the UPR in donor cells did not result in UPR transmission to acceptor cells. Moreover, no transmission was detected upon full UPR activation by nutrient deprivation or inducible expression of the heavy chain of immunoglobulin M in donor HeLa cells. In addition, in direct co‐culture of donor cells expressing the immunoglobulin M heavy chain and fluorescent UPR reporter acceptor HeLa cells, UPR transmission was not observed. In conclusion, carry‐over of pharmaca is a major confounding factor in pharmaca‐based UPR transmission protocols that are therefore unsuitable to study cell‐to‐cell UPR transmission. In addition, the absence of UPR transmission in non‐pharmaca‐based models of UPR activation indicates that cell‐to‐cell UPR transmission does not occur in cell culture. [ABSTRACT FROM AUTHOR]

Published
2020
Full Text
View/download PDF

37. ER ‐to‐lysosome‐associated degradation of proteasome‐resistant ATZ polymers occurs via receptor‐mediated vesicular transport

Author

Fregno, Ilaria, primary, Fasana, Elisa, additional, Bergmann, Timothy J, additional, Raimondi, Andrea, additional, Loi, Marisa, additional, Soldà, Tatiana, additional, Galli, Carmela, additional, D'Antuono, Rocco, additional, Morone, Diego, additional, Danieli, Alberto, additional, Paganetti, Paolo, additional, Anken, Eelco, additional, and Molinari, Maurizio, additional

Published
2018
Full Text
View/download PDF

39. A RIDDle solved: why an intact IRE1α/XBP-1 signaling relay is key for humoral immune responses

Author

van Anken E1, Orsi A, SITIA , ROBERTO, VAN ANKEN, EELCO, van Anken, E1, Orsi, A, Sitia, Roberto, and VAN ANKEN, Eelco

Abstract

As they commit to plasma cell differentiation, B lymphocytes must swiftly gear up to produce and secrete huge amounts of antibodies. To develop their secretory capacity, B cells exploit a signaling pathway that is employed by all eukaryotic cells in response to endoplasmic reticulum stress. An article by Benhamron et al. in this issue of the European Journal of Immunology, [Eur. J. Immunol. 2014. 44: 867-876] sheds new light on why an intact IRE1/XBP-1 signaling relay is central to orchestrate the full-blown expansion of the secretory machinery needed for massive antibody production.

Published
2014

40. mRNA Targeting to ER Stress Signaling Sites

Author

Aragón, Tomás, van Anken, Eelco, Pincus, David, Serafimova, Iana M., Korennykh, Alexei V., Rubio, Claudia A., and Walter, Peter

Subjects
Article
Abstract

Deficiencies in the protein folding capacity of the endoplasmic reticulum (ER) in all eucaryotic cells lead to ER stress and triggers the unfolded protein response (UPR)1–3. ER stress is sensed by Ire1, a transmembrane kinase/endoribonuclease, which initiates the non-conventional splicing of the mRNA encoding a key transcription activator, Hac1 in yeast or XBP-1 in metazoans. In the absence of ER stress, ribosomes are stalled on unspliced HAC1 mRNA. The translational control is imposed by a base pairing interaction between the HAC1 intron and the HAC1 5′ untranslated region (5′UTR)4. After excision of the intron, tRNA ligase joins the severed exons5,6, lifting the translational block and allowing synthesis of Hac1 from the spliced HAC1 mRNA to ensue4. Hac1 in turn drives the UPR gene expression program comprising 7–8% of the yeast genome7 to counteract ER stress. We show here that upon activation, Ire1 molecules cluster in the ER membrane into discrete foci of higher-order oligomers, to which unspliced HAC1 mRNA is recruited by means of a conserved bipartite targeting element contained in the 3′ untranslated region (3′UTR). Disruption of either Ire1 clustering or of HAC1 mRNA recruitment impairs UPR signaling. The HAC1 3′UTR element is sufficient to target other mRNAs to Ire1 foci, as long as their translation is repressed. Translational repression afforded by the intron fulfills this requirement for HAC1 mRNA. Recruitment of mRNA to signaling centers provides a new paradigm for the control of eukaryotic gene expression.

Published
2008

44. Iron affects Ire1 clustering propensity and the amplitude of endoplasmic reticulum stress signaling

Author

Cohen, Nir, primary, Breker, Michal, additional, Bakunts, Anush, additional, Pesek, Kristina, additional, Chas, Ainara, additional, Argemí, Josepmaria, additional, Orsi, Andrea, additional, Gal, Lihi, additional, Chuartzman, Silvia, additional, Wigelman, Yoav, additional, Jonas, Felix, additional, Walter, Peter, additional, Ernst, Robert, additional, Aragón, Tomás, additional, van Anken, Eelco, additional, and Schuldiner, Maya, additional

Published
2017
Full Text
View/download PDF

45. Missing Links in Antibody Assembly Control

Author

Anelli, Tiziana and van Anken, Eelco

Subjects
Article Subject
Abstract

Fidelity of the humoral immune response requires that quiescent B lymphocytes display membrane bound immunoglobulin M (IgM) on B lymphocytes surface as part of the B cell receptor, whose function is to recognize an antigen. At the same time B lymphocytes should not secrete IgM until recognition of the antigen has occurred. The heavy chains of the secretory IgM have a C-terminal tail with a cysteine instead of a membrane anchor, which serves to covalently link the IgM subunits by disulfide bonds to form “pentamers” or “hexamers.” By virtue of the same cysteine, unassembled secretory IgM subunits are recognized and retained (via mixed disulfide bonds) by members of the protein disulfide isomerase family, in particular ERp44. This so-called “thiol-mediated retention” bars assembly intermediates from prematurely leaving the cell and thereby exerts quality control on the humoral immune response. In this essay we discuss recent findings on how ERp44 governs such assembly control in a pH-dependent manner, shuttling between the cisGolgi and endoplasmic reticulum, and finally on how pERp1/MZB1, possibly as a co-chaperone of GRP94, may help to overrule the thiol-mediated retention in the activated B cell to give way to antibody secretion.

Published
2013
Full Text
View/download PDF

46. The intellectual disability protein RAB39B selectively regulates GluA2 trafficking to determine synaptic AMPAR composition

Author

Mignogna, Maria Lidia, primary, Giannandrea, Maila, additional, Gurgone, Antonia, additional, Fanelli, Francesca, additional, Raimondi, Francesco, additional, Mapelli, Lisa, additional, Bassani, Silvia, additional, Fang, Huaqiang, additional, Van Anken, Eelco, additional, Alessio, Massimo, additional, Passafaro, Maria, additional, Gatti, Silvia, additional, Esteban, José A., additional, Huganir, Richard, additional, and D’Adamo, Patrizia, additional

Published
2015
Full Text
View/download PDF

Catalog

Books, media, physical & digital resources
See catalog results