Journal
JOURNAL OF CELL BIOLOGY
Volume 189, Issue 7, Pages 1107-1115Publisher
ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.201001149
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Funding
- American Institute for Cancer Research [06-0528]
- Dutch Foundation for Cancer Research (KWF) [2006-3714]
- National Institutes of Health [GM 072744]
- National Science Foundation (Chemical, Bioengineering, Environmental, and Transport Systems) [0853705]
- Div Of Chem, Bioeng, Env, & Transp Sys
- Directorate For Engineering [0853705] Funding Source: National Science Foundation
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C ell 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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