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The Arp1/11 minifilament of dynactin primes the endosomal Arp2/3 complex
Dendritic actin networks develop from a first actin filament through branching by the Arp2/3 complex. At the surface of endosomes, the WASH complex activates the Arp2/3 complex and interacts with the capping protein for unclear reasons. Here, we show that the WASH complex interacts with dynactin and...
Autores principales: | , , , , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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American Association for the Advancement of Science
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7806238/ https://www.ncbi.nlm.nih.gov/pubmed/33523880 http://dx.doi.org/10.1126/sciadv.abd5956 |
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author | Fokin, Artem I. David, Violaine Oguievetskaia, Ksenia Derivery, Emmanuel Stone, Caroline E. Cao, Luyan Rocques, Nathalie Molinie, Nicolas Henriot, Véronique Aumont-Nicaise, Magali Hinckelmann, Maria-Victoria Saudou, Frédéric Le Clainche, Christophe Carter, Andrew P. Romet-Lemonne, Guillaume Gautreau, Alexis M. |
author_facet | Fokin, Artem I. David, Violaine Oguievetskaia, Ksenia Derivery, Emmanuel Stone, Caroline E. Cao, Luyan Rocques, Nathalie Molinie, Nicolas Henriot, Véronique Aumont-Nicaise, Magali Hinckelmann, Maria-Victoria Saudou, Frédéric Le Clainche, Christophe Carter, Andrew P. Romet-Lemonne, Guillaume Gautreau, Alexis M. |
author_sort | Fokin, Artem I. |
collection | PubMed |
description | Dendritic actin networks develop from a first actin filament through branching by the Arp2/3 complex. At the surface of endosomes, the WASH complex activates the Arp2/3 complex and interacts with the capping protein for unclear reasons. Here, we show that the WASH complex interacts with dynactin and uncaps it through its FAM21 subunit. In vitro, the uncapped Arp1/11 minifilament elongates an actin filament, which then primes the WASH-induced Arp2/3 branching reaction. In dynactin-depleted cells or in cells where the WASH complex is reconstituted with a FAM21 mutant that cannot uncap dynactin, formation of branched actin at the endosomal surface is impaired. Our results reveal the importance of the WASH complex in coordinating two complexes containing actin-related proteins. |
format | Online Article Text |
id | pubmed-7806238 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | American Association for the Advancement of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-78062382021-01-21 The Arp1/11 minifilament of dynactin primes the endosomal Arp2/3 complex Fokin, Artem I. David, Violaine Oguievetskaia, Ksenia Derivery, Emmanuel Stone, Caroline E. Cao, Luyan Rocques, Nathalie Molinie, Nicolas Henriot, Véronique Aumont-Nicaise, Magali Hinckelmann, Maria-Victoria Saudou, Frédéric Le Clainche, Christophe Carter, Andrew P. Romet-Lemonne, Guillaume Gautreau, Alexis M. Sci Adv Research Articles Dendritic actin networks develop from a first actin filament through branching by the Arp2/3 complex. At the surface of endosomes, the WASH complex activates the Arp2/3 complex and interacts with the capping protein for unclear reasons. Here, we show that the WASH complex interacts with dynactin and uncaps it through its FAM21 subunit. In vitro, the uncapped Arp1/11 minifilament elongates an actin filament, which then primes the WASH-induced Arp2/3 branching reaction. In dynactin-depleted cells or in cells where the WASH complex is reconstituted with a FAM21 mutant that cannot uncap dynactin, formation of branched actin at the endosomal surface is impaired. Our results reveal the importance of the WASH complex in coordinating two complexes containing actin-related proteins. American Association for the Advancement of Science 2021-01-13 /pmc/articles/PMC7806238/ /pubmed/33523880 http://dx.doi.org/10.1126/sciadv.abd5956 Text en Copyright © 2021 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works. Distributed under a Creative Commons Attribution NonCommercial License 4.0 (CC BY-NC). https://creativecommons.org/licenses/by-nc/4.0/ https://creativecommons.org/licenses/by-nc/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution-NonCommercial license (https://creativecommons.org/licenses/by-nc/4.0/) , which permits use, distribution, and reproduction in any medium, so long as the resultant use is not for commercial advantage and provided the original work is properly cited. |
spellingShingle | Research Articles Fokin, Artem I. David, Violaine Oguievetskaia, Ksenia Derivery, Emmanuel Stone, Caroline E. Cao, Luyan Rocques, Nathalie Molinie, Nicolas Henriot, Véronique Aumont-Nicaise, Magali Hinckelmann, Maria-Victoria Saudou, Frédéric Le Clainche, Christophe Carter, Andrew P. Romet-Lemonne, Guillaume Gautreau, Alexis M. The Arp1/11 minifilament of dynactin primes the endosomal Arp2/3 complex |
title | The Arp1/11 minifilament of dynactin primes the endosomal Arp2/3 complex |
title_full | The Arp1/11 minifilament of dynactin primes the endosomal Arp2/3 complex |
title_fullStr | The Arp1/11 minifilament of dynactin primes the endosomal Arp2/3 complex |
title_full_unstemmed | The Arp1/11 minifilament of dynactin primes the endosomal Arp2/3 complex |
title_short | The Arp1/11 minifilament of dynactin primes the endosomal Arp2/3 complex |
title_sort | arp1/11 minifilament of dynactin primes the endosomal arp2/3 complex |
topic | Research Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7806238/ https://www.ncbi.nlm.nih.gov/pubmed/33523880 http://dx.doi.org/10.1126/sciadv.abd5956 |
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