Artículo
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
Fecha de publicación:
12/2018
Editorial:
Nature Publishing Group
Revista:
Nature Communications
ISSN:
2041-1723
Idioma:
Inglés
Tipo de recurso:
Artículo publicado
Clasificación temática:
Resumen
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.
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Identificadores
Colecciones
Articulos(CCT - MENDOZA)
Articulos de CTRO.CIENTIFICO TECNOL.CONICET - MENDOZA
Articulos de CTRO.CIENTIFICO TECNOL.CONICET - MENDOZA
Citación
Baschieri, Francesco; Dayot, Stéphane; Elkhatib, Nadia; Ly, Nathalie; Capmany, Anahi; et al.; Frustrated endocytosis controls contractility-independent mechanotransduction at clathrin-coated structures; Nature Publishing Group; Nature Communications; 9; 1; 12-2018
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