α-catenin cytomechanics--role in cadherin-dependent adhesion and mechanotransduction

J Cell Sci. 2014 Apr 15;127(Pt 8):1779-91. doi: 10.1242/jcs.139014. Epub 2014 Feb 12.

Abstract

The findings presented here demonstrate the role of α-catenin in cadherin-based adhesion and mechanotransduction in different mechanical contexts. Bead-twisting measurements in conjunction with imaging, and the use of different cell lines and α-catenin mutants reveal that the acute local mechanical manipulation of cadherin bonds triggers vinculin and actin recruitment to cadherin adhesions in an actin- and α-catenin-dependent manner. The modest effect of α-catenin on the two-dimensional binding affinities of cell surface cadherins further suggests that force-activated adhesion strengthening is due to enhanced cadherin-cytoskeletal interactions rather than to α-catenin-dependent affinity modulation. Complementary investigations of cadherin-based rigidity sensing also suggest that, although α-catenin alters traction force generation, it is not the sole regulator of cell contractility on compliant cadherin-coated substrata.

Keywords: Adhesion; Cadherin; Mechanotransduction; α-Catenin.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Actins / metabolism
  • Animals
  • Binding Sites
  • Biomechanical Phenomena
  • Cadherins / blood*
  • Cadherins / chemistry
  • Cadherins / physiology*
  • Cell Adhesion*
  • Cell Line, Tumor
  • Dogs
  • Erythrocytes / metabolism
  • Humans
  • Kinetics
  • Madin Darby Canine Kidney Cells
  • Mechanotransduction, Cellular*
  • Protein Interaction Domains and Motifs
  • Protein Transport
  • Vinculin / metabolism
  • alpha Catenin / physiology*

Substances

  • Actins
  • Cadherins
  • alpha Catenin
  • Vinculin