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Polarity protein Par3 controls B-cell receptor dynamics and antigen extraction at the immune synapse

B-cell receptor (BCR) engagement with surface-tethered antigens leads to the formation of an immune synapse, which facilitates antigen uptake for presentation to T-lymphocytes. Antigen internalization and processing rely on the early dynein-dependent transport of BCR–antigen microclusters to the syn...

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Autores principales: Reversat, Anne, Yuseff, Maria-Isabel, Lankar, Danielle, Malbec, Odile, Obino, Dorian, Maurin, Mathieu, Penmatcha, Naga Venkata Gayathri, Amoroso, Alejandro, Sengmanivong, Lucie, Gundersen, Gregg G., Mellman, Ira, Darchen, François, Desnos, Claire, Pierobon, Paolo, Lennon-Duménil, Ana-Maria
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The American Society for Cell Biology 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4454175/
https://www.ncbi.nlm.nih.gov/pubmed/25631815
http://dx.doi.org/10.1091/mbc.E14-09-1373
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author Reversat, Anne
Yuseff, Maria-Isabel
Lankar, Danielle
Malbec, Odile
Obino, Dorian
Maurin, Mathieu
Penmatcha, Naga Venkata Gayathri
Amoroso, Alejandro
Sengmanivong, Lucie
Gundersen, Gregg G.
Mellman, Ira
Darchen, François
Desnos, Claire
Pierobon, Paolo
Lennon-Duménil, Ana-Maria
author_facet Reversat, Anne
Yuseff, Maria-Isabel
Lankar, Danielle
Malbec, Odile
Obino, Dorian
Maurin, Mathieu
Penmatcha, Naga Venkata Gayathri
Amoroso, Alejandro
Sengmanivong, Lucie
Gundersen, Gregg G.
Mellman, Ira
Darchen, François
Desnos, Claire
Pierobon, Paolo
Lennon-Duménil, Ana-Maria
author_sort Reversat, Anne
collection PubMed
description B-cell receptor (BCR) engagement with surface-tethered antigens leads to the formation of an immune synapse, which facilitates antigen uptake for presentation to T-lymphocytes. Antigen internalization and processing rely on the early dynein-dependent transport of BCR–antigen microclusters to the synapse center, as well as on the later polarization of the microtubule-organizing center (MTOC). MTOC repositioning allows the release of proteases and the delivery of MHC class II molecules at the synapse. Whether and how these events are coordinated have not been addressed. Here we show that the ancestral polarity protein Par3 promotes BCR–antigen microcluster gathering, as well as MTOC polarization and lysosome exocytosis, at the synapse by facilitating local dynein recruitment. Par3 is also required for antigen presentation to T-lymphocytes. Par3 therefore emerges as a key molecule in the coupling of the early and late events needed for efficient extraction and processing of immobilized antigen by B-cells.
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spelling pubmed-44541752015-06-16 Polarity protein Par3 controls B-cell receptor dynamics and antigen extraction at the immune synapse Reversat, Anne Yuseff, Maria-Isabel Lankar, Danielle Malbec, Odile Obino, Dorian Maurin, Mathieu Penmatcha, Naga Venkata Gayathri Amoroso, Alejandro Sengmanivong, Lucie Gundersen, Gregg G. Mellman, Ira Darchen, François Desnos, Claire Pierobon, Paolo Lennon-Duménil, Ana-Maria Mol Biol Cell Articles B-cell receptor (BCR) engagement with surface-tethered antigens leads to the formation of an immune synapse, which facilitates antigen uptake for presentation to T-lymphocytes. Antigen internalization and processing rely on the early dynein-dependent transport of BCR–antigen microclusters to the synapse center, as well as on the later polarization of the microtubule-organizing center (MTOC). MTOC repositioning allows the release of proteases and the delivery of MHC class II molecules at the synapse. Whether and how these events are coordinated have not been addressed. Here we show that the ancestral polarity protein Par3 promotes BCR–antigen microcluster gathering, as well as MTOC polarization and lysosome exocytosis, at the synapse by facilitating local dynein recruitment. Par3 is also required for antigen presentation to T-lymphocytes. Par3 therefore emerges as a key molecule in the coupling of the early and late events needed for efficient extraction and processing of immobilized antigen by B-cells. The American Society for Cell Biology 2015-04-01 /pmc/articles/PMC4454175/ /pubmed/25631815 http://dx.doi.org/10.1091/mbc.E14-09-1373 Text en © 2015 Reversat, Yuseff, et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0). “ASCB®,” “The American Society for Cell Biology®,” and “Molecular Biology of the Cell®” are registered trademarks of The American Society for Cell Biology.
spellingShingle Articles
Reversat, Anne
Yuseff, Maria-Isabel
Lankar, Danielle
Malbec, Odile
Obino, Dorian
Maurin, Mathieu
Penmatcha, Naga Venkata Gayathri
Amoroso, Alejandro
Sengmanivong, Lucie
Gundersen, Gregg G.
Mellman, Ira
Darchen, François
Desnos, Claire
Pierobon, Paolo
Lennon-Duménil, Ana-Maria
Polarity protein Par3 controls B-cell receptor dynamics and antigen extraction at the immune synapse
title Polarity protein Par3 controls B-cell receptor dynamics and antigen extraction at the immune synapse
title_full Polarity protein Par3 controls B-cell receptor dynamics and antigen extraction at the immune synapse
title_fullStr Polarity protein Par3 controls B-cell receptor dynamics and antigen extraction at the immune synapse
title_full_unstemmed Polarity protein Par3 controls B-cell receptor dynamics and antigen extraction at the immune synapse
title_short Polarity protein Par3 controls B-cell receptor dynamics and antigen extraction at the immune synapse
title_sort polarity protein par3 controls b-cell receptor dynamics and antigen extraction at the immune synapse
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4454175/
https://www.ncbi.nlm.nih.gov/pubmed/25631815
http://dx.doi.org/10.1091/mbc.E14-09-1373
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