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Annu Rev Cell Dev Biol. 2014;30:291-315. doi: 10.1146/annurev-cellbio-100913-013212. Epub 2014 Jul 9.

Cadherin adhesion and mechanotransduction.

Author information

1
Departments of Chemical and Biomolecular Engineering, Chemistry, and Biochemistry, University of Illinois, Urbana, Illinois 61801; email: leckband@illinois.edu.

Abstract

Cadherins are the principal adhesion proteins at intercellular junctions and function as the biochemical Velcro that binds cells together. Besides this mechanical function, cadherin complexes are also mechanotransducers that sense changes in tension and trigger adaptive reinforcement of intercellular junctions. The assembly and regulation of cadherin adhesions are central to their mechanical functions, and new evidence is presented for a comprehensive model of cadherin adhesion, which is surprisingly more complex than previously appreciated. Recent findings also shed new light on mechanisms that regulate cadherin junction assembly, adhesion, and mechanotransduction. We further describe recent evidence for cadherin-based mechanotransduction, and the rudiments of the molecular mechanism, which involves α-catenin and vinculin as key elements. Potential roles of a broader cast of possible force-sensitive partners are considered, as well as known and speculative biological consequences of adhesion and force transduction at cadherin-mediated junctions.

KEYWORDS:

actin; allostery; cytoskeleton; morphogenesis; α-catenin

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