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Frustrated endocytosis controls contractility-independent mechanotransduction at clathrin-coated structures
It is generally assumed that cells interrogate the mechanical properties of their environment by pushing and pulling on the extracellular matrix (ECM). For instance, acto-myosin-dependent contraction forces exerted at focal adhesions (FAs) allow the cell to actively probe substrate elasticity. Here,...
Autores principales: | , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2018
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6148028/ https://www.ncbi.nlm.nih.gov/pubmed/30237420 http://dx.doi.org/10.1038/s41467-018-06367-y |
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author | Baschieri, Francesco Dayot, Stéphane Elkhatib, Nadia Ly, Nathalie Capmany, Anahi Schauer, Kristine Betz, Timo Vignjevic, Danijela Matic Poincloux, Renaud Montagnac, Guillaume |
author_facet | Baschieri, Francesco Dayot, Stéphane Elkhatib, Nadia Ly, Nathalie Capmany, Anahi Schauer, Kristine Betz, Timo Vignjevic, Danijela Matic Poincloux, Renaud Montagnac, Guillaume |
author_sort | Baschieri, Francesco |
collection | PubMed |
description | It is generally assumed that cells interrogate the mechanical properties of their environment by pushing and pulling on the extracellular matrix (ECM). For instance, acto-myosin-dependent contraction forces exerted at focal adhesions (FAs) allow the cell to actively probe substrate elasticity. Here, we report that a subset of long-lived and flat clathrin-coated structures (CCSs), also termed plaques, are contractility-independent mechanosensitive signaling platforms. We observed that plaques assemble in response to increasing substrate rigidity and that this is independent of FAs, actin and myosin-II activity. We show that plaque assembly depends on αvβ5 integrin, and is a consequence of frustrated endocytosis whereby αvβ5 tightly engaged with the stiff substrate locally stalls CCS dynamics. We also report that plaques serve as platforms for receptor-dependent signaling and are required for increased Erk activation and cell proliferation on stiff environments. We conclude that CCSs are mechanotransduction structures that sense substrate rigidity independently of cell contractility. |
format | Online Article Text |
id | pubmed-6148028 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-61480282018-09-25 Frustrated endocytosis controls contractility-independent mechanotransduction at clathrin-coated structures Baschieri, Francesco Dayot, Stéphane Elkhatib, Nadia Ly, Nathalie Capmany, Anahi Schauer, Kristine Betz, Timo Vignjevic, Danijela Matic Poincloux, Renaud Montagnac, Guillaume Nat Commun Article It is generally assumed that cells interrogate the mechanical properties of their environment by pushing and pulling on the extracellular matrix (ECM). For instance, acto-myosin-dependent contraction forces exerted at focal adhesions (FAs) allow the cell to actively probe substrate elasticity. Here, we report that a subset of long-lived and flat clathrin-coated structures (CCSs), also termed plaques, are contractility-independent mechanosensitive signaling platforms. We observed that plaques assemble in response to increasing substrate rigidity and that this is independent of FAs, actin and myosin-II activity. We show that plaque assembly depends on αvβ5 integrin, and is a consequence of frustrated endocytosis whereby αvβ5 tightly engaged with the stiff substrate locally stalls CCS dynamics. We also report that plaques serve as platforms for receptor-dependent signaling and are required for increased Erk activation and cell proliferation on stiff environments. We conclude that CCSs are mechanotransduction structures that sense substrate rigidity independently of cell contractility. Nature Publishing Group UK 2018-09-20 /pmc/articles/PMC6148028/ /pubmed/30237420 http://dx.doi.org/10.1038/s41467-018-06367-y Text en © The Author(s) 2018 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/. |
spellingShingle | Article Baschieri, Francesco Dayot, Stéphane Elkhatib, Nadia Ly, Nathalie Capmany, Anahi Schauer, Kristine Betz, Timo Vignjevic, Danijela Matic Poincloux, Renaud Montagnac, Guillaume Frustrated endocytosis controls contractility-independent mechanotransduction at clathrin-coated structures |
title | Frustrated endocytosis controls contractility-independent mechanotransduction at clathrin-coated structures |
title_full | Frustrated endocytosis controls contractility-independent mechanotransduction at clathrin-coated structures |
title_fullStr | Frustrated endocytosis controls contractility-independent mechanotransduction at clathrin-coated structures |
title_full_unstemmed | Frustrated endocytosis controls contractility-independent mechanotransduction at clathrin-coated structures |
title_short | Frustrated endocytosis controls contractility-independent mechanotransduction at clathrin-coated structures |
title_sort | frustrated endocytosis controls contractility-independent mechanotransduction at clathrin-coated structures |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6148028/ https://www.ncbi.nlm.nih.gov/pubmed/30237420 http://dx.doi.org/10.1038/s41467-018-06367-y |
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