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Vinculin potentiates E-cadherin mechanosensing and is recruited to actin-anchored sites within adherens junctions in a myosin II–dependent manner

Cell surface receptors integrate chemical and mechanical cues to regulate a wide range of biological processes. Integrin complexes are the mechanotransducers between the extracellular matrix and the actomyosin cytoskeleton. By analogy, cadherin complexes may function as mechanosensors at cell–cell j...

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Detalles Bibliográficos
Autores principales: le Duc, Quint, Shi, Quanming, Blonk, Iris, Sonnenberg, Arnoud, Wang, Ning, Leckband, Deborah, de Rooij, Johan
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 2010
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2894457/
https://www.ncbi.nlm.nih.gov/pubmed/20584916
http://dx.doi.org/10.1083/jcb.201001149
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author le Duc, Quint
Shi, Quanming
Blonk, Iris
Sonnenberg, Arnoud
Wang, Ning
Leckband, Deborah
de Rooij, Johan
author_facet le Duc, Quint
Shi, Quanming
Blonk, Iris
Sonnenberg, Arnoud
Wang, Ning
Leckband, Deborah
de Rooij, Johan
author_sort le Duc, Quint
collection PubMed
description Cell surface receptors integrate chemical and mechanical cues to regulate a wide range of biological processes. Integrin complexes are the mechanotransducers between the extracellular matrix and the actomyosin cytoskeleton. By analogy, cadherin complexes may function as mechanosensors at cell–cell junctions, but this capacity of cadherins has not been directly demonstrated. Furthermore, the molecular composition of the link between E-cadherin and actin, which is needed to sustain such a function, is unresolved. In this study, we describe nanomechanical measurements demonstrating that E-cadherin complexes are functional mechanosensors that transmit force between F-actin and E-cadherin. Imaging experiments reveal that intercellular forces coincide with vinculin accumulation at actin-anchored cadherin adhesions, and nanomechanical measurements show that vinculin potentiates the E-cadherin mechanosensory response. These investigations directly demonstrate the mechanosensory capacity of the E-cadherin complex and identify a novel function for vinculin at cell–cell junctions. These findings have implications for barrier function, morphogenesis, cell migration, and invasion and may extend to all soft tissues in which classical cadherins regulate cell–cell adhesion.
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spelling pubmed-28944572010-12-28 Vinculin potentiates E-cadherin mechanosensing and is recruited to actin-anchored sites within adherens junctions in a myosin II–dependent manner le Duc, Quint Shi, Quanming Blonk, Iris Sonnenberg, Arnoud Wang, Ning Leckband, Deborah de Rooij, Johan J Cell Biol Research Articles Cell surface receptors integrate chemical and mechanical cues to regulate a wide range of biological processes. Integrin complexes are the mechanotransducers between the extracellular matrix and the actomyosin cytoskeleton. By analogy, cadherin complexes may function as mechanosensors at cell–cell junctions, but this capacity of cadherins has not been directly demonstrated. Furthermore, the molecular composition of the link between E-cadherin and actin, which is needed to sustain such a function, is unresolved. In this study, we describe nanomechanical measurements demonstrating that E-cadherin complexes are functional mechanosensors that transmit force between F-actin and E-cadherin. Imaging experiments reveal that intercellular forces coincide with vinculin accumulation at actin-anchored cadherin adhesions, and nanomechanical measurements show that vinculin potentiates the E-cadherin mechanosensory response. These investigations directly demonstrate the mechanosensory capacity of the E-cadherin complex and identify a novel function for vinculin at cell–cell junctions. These findings have implications for barrier function, morphogenesis, cell migration, and invasion and may extend to all soft tissues in which classical cadherins regulate cell–cell adhesion. The Rockefeller University Press 2010-06-28 /pmc/articles/PMC2894457/ /pubmed/20584916 http://dx.doi.org/10.1083/jcb.201001149 Text en © 2010 le Duc et al. This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/).
spellingShingle Research Articles
le Duc, Quint
Shi, Quanming
Blonk, Iris
Sonnenberg, Arnoud
Wang, Ning
Leckband, Deborah
de Rooij, Johan
Vinculin potentiates E-cadherin mechanosensing and is recruited to actin-anchored sites within adherens junctions in a myosin II–dependent manner
title Vinculin potentiates E-cadherin mechanosensing and is recruited to actin-anchored sites within adherens junctions in a myosin II–dependent manner
title_full Vinculin potentiates E-cadherin mechanosensing and is recruited to actin-anchored sites within adherens junctions in a myosin II–dependent manner
title_fullStr Vinculin potentiates E-cadherin mechanosensing and is recruited to actin-anchored sites within adherens junctions in a myosin II–dependent manner
title_full_unstemmed Vinculin potentiates E-cadherin mechanosensing and is recruited to actin-anchored sites within adherens junctions in a myosin II–dependent manner
title_short Vinculin potentiates E-cadherin mechanosensing and is recruited to actin-anchored sites within adherens junctions in a myosin II–dependent manner
title_sort vinculin potentiates e-cadherin mechanosensing and is recruited to actin-anchored sites within adherens junctions in a myosin ii–dependent manner
topic Research Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2894457/
https://www.ncbi.nlm.nih.gov/pubmed/20584916
http://dx.doi.org/10.1083/jcb.201001149
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