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• W2891465278 abstract "Abstract 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." @default.
• W2891465278 created "2018-09-27" @default.
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• W2891465278 date "2018-09-20" @default.
• W2891465278 modified "2023-10-04" @default.
• W2891465278 title "Frustrated endocytosis controls contractility-independent mechanotransduction at clathrin-coated structures" @default.
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• W2891465278 doi "https://doi.org/10.1038/s41467-018-06367-y" @default.
• W2891465278 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6148028" @default.
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• W2891465278 hasPublicationYear "2018" @default.
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