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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...
Autores principales: | , , , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The American Society for Cell Biology
2015
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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. |
format | Online Article Text |
id | pubmed-4454175 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | The American Society for Cell Biology |
record_format | MEDLINE/PubMed |
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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