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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. / le Duc, Q.; Shi, Q.; Blonk, I.; Sonnenberg, A.; Wang, N.; Leckband, D.; de Rooij, J.

In: Journal of Cell Biology, Vol. 189, No. 7, 2010, p. 1107-1115.

Research output: Scientific - peer-reviewArticle

Harvard

le Duc, Q, Shi, Q, Blonk, I, Sonnenberg, A, Wang, N, Leckband, D & de Rooij, J 2010, 'Vinculin potentiates E-cadherin mechanosensing and is recruited to actin-anchored sites within adherens junctions in a myosin II-dependent manner' Journal of Cell Biology, vol 189, no. 7, pp. 1107-1115. DOI: 10.1083/jcb.201001149

APA

le Duc, Q., Shi, Q., Blonk, I., Sonnenberg, A., Wang, N., Leckband, D., & de Rooij, J. (2010). Vinculin potentiates E-cadherin mechanosensing and is recruited to actin-anchored sites within adherens junctions in a myosin II-dependent manner. Journal of Cell Biology, 189(7), 1107-1115. DOI: 10.1083/jcb.201001149

Vancouver

le Duc Q, Shi Q, Blonk I, Sonnenberg A, Wang N, Leckband D et al. Vinculin potentiates E-cadherin mechanosensing and is recruited to actin-anchored sites within adherens junctions in a myosin II-dependent manner. Journal of Cell Biology. 2010;189(7):1107-1115. Available from, DOI: 10.1083/jcb.201001149

Author

le Duc, Q.; Shi, Q.; Blonk, I.; Sonnenberg, A.; Wang, N.; Leckband, D.; de Rooij, J. / Vinculin potentiates E-cadherin mechanosensing and is recruited to actin-anchored sites within adherens junctions in a myosin II-dependent manner.

In: Journal of Cell Biology, Vol. 189, No. 7, 2010, p. 1107-1115.

Research output: Scientific - peer-reviewArticle

BibTeX

@article{6fe2f5f491ca49d3830e6de10e11a1b4,
title = "Vinculin potentiates E-cadherin mechanosensing and is recruited to actin-anchored sites within adherens junctions in a myosin II-dependent manner",
abstract = "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.",
author = "{le Duc}, Q. and Q. Shi and I. Blonk and A. Sonnenberg and N. Wang and D. Leckband and {de Rooij}, J.",
note = "Reporting year: 2010 Metis note: 2894457; jcb.201001149 [pii]",
year = "2010",
doi = "10.1083/jcb.201001149",
volume = "189",
pages = "1107--1115",
journal = "Journal of Cell Biology",
issn = "0021-9525",
publisher = "Rockefeller University Press",
number = "7",

}

RIS

TY - JOUR

T1 - Vinculin potentiates E-cadherin mechanosensing and is recruited to actin-anchored sites within adherens junctions in a myosin II-dependent manner

AU - le Duc,Q.

AU - Shi,Q.

AU - Blonk,I.

AU - Sonnenberg,A.

AU - Wang,N.

AU - Leckband,D.

AU - de Rooij,J.

N1 - Reporting year: 2010 Metis note: 2894457; jcb.201001149 [pii]

PY - 2010

Y1 - 2010

N2 - 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.

AB - 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.

U2 - 10.1083/jcb.201001149

DO - 10.1083/jcb.201001149

M3 - Article

VL - 189

SP - 1107

EP - 1115

JO - Journal of Cell Biology

T2 - Journal of Cell Biology

JF - Journal of Cell Biology

SN - 0021-9525

IS - 7

ER -

ID: 273829