Cited by 652Cellular Mechanics and InteractionsCell Adhesion Molecules ResearchSkin and Cellular Biology Research

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

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le Duc, Quint, Shi, Quanming, Blonk, Iris, Sonnenberg, Arnoud, Wang, Ning, Leckband, Deborah, de Rooij, Johan·2010·Journal of Cell Biology

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.

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Authors
le Duc, Q., Shi, Q., Blonk, I., Sonnenberg, A., Wang, N., Leckband, D., & de Rooij, J.
Affiliations
  • Hubrecht Institute, University Medical Centre Utrecht, 3584 CT Utrecht, Netherlands 1
  • University of Illinois Urbana-Champaign (US)
  • University Medical Center Utrecht (NL)
  • The Netherlands Cancer Institute (NL)
Corresponding author
  • Wang, Ning
  • Leckband, Deborah
Venue
Journal of Cell Biology
Published
2010-06-28
Volume
189
Issue
7
Pages
1107-1115
ISSN
  • 0021-9525 (ISSN-L)
  • 1540-8140
OpenAlex
W2139731224
Cited by
652
References
2
Citations by year
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FWCI
20.85
Type
journal article
Language
en
Open access
Licence
cc-by-nc-sa
Locations
  • The Journal of Cell Biology (publishedVersion, cc-by-nc-sa)
  • PubMed Central (publishedVersion, cc-by-nc-sa)
  • PubMed (publishedVersion)
  • Data Archiving and Networked Services (DANS) (submittedVersion)
  • KNAW Research Portal (The Royal Netherlands Academy of Arts and Sciences) (submittedVersion)
Funders
National Institute of General Medical Sciences (R01GM097443, GM072744, R01GM072744)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular Mechanics and Interactions
  • Health Sciences › Medicine › Immunology and Allergy › Cell Adhesion Molecules Research
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Skin and Cellular Biology Research
Keywords
E-cadherin, vinculin, mechanosensing, adherens junctions, myosin II, cell-cell adhesion, actin cytoskeleton, cell migration, barrier function
MeSH terms
Actins, Animals, Cell Adhesion, Dogs, Humans, Insecta, Cadherins, Vinculin, Protein Transport, Adherens Junctions, Myosin Type II, Mechanotransduction, Cellular, Multiprotein Complexes

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