α-Catenin cytomechanics – role in cadherin-dependent adhesion and mechanotransduction

Author:

Barry Adrienne K.12,Tabdili Hamid3,Muhamed Ismaeel1,Wu Jun3,Shashikanth Nitesh1,Gomez Guillermo A.4,Yap Alpha S.4,Gottardi Cara J.5,de Rooij Johan6,Wang Ning7,Leckband Deborah E.13

Affiliation:

1. Department of Biochemistry, University of Illinois, Urbana, IL 61801-3709, USA

2. Medical Scholars Program, University of Illinois, Urbana, IL 61801-3709, USA

3. Department of Chemical and Biomolecular Engineering, University of Illinois, Urbana, IL 61801-3709, USA

4. Division of Molecular Cell Biology, Institute for Molecular Bioscience, University of Queensland, St. Lucia, Brisbane, QLD 4072, Australia

5. Northwestern University College of Medicine, Chicago, IL 60611, USA

6. Hubrecht Institute for Developmental Biology and Stem Cell Research, University Medical Center Utrecht, 3584 CT, Utrecht, Netherlands

7. Department of Mechanical Engineering, University of Illinois, Urbana, IL 61801-3709, USA

Abstract

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.

Publisher

The Company of Biologists

Subject

Cell Biology

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