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

TY - JOUR

T1 - α-catenin cytomechanics--role in cadherin-dependent adhesion and mechanotransduction

AU - Barry, Adrienne K

AU - Tabdili, Hamid

AU - Muhamed, Ismaeel

AU - Wu, Jun

AU - Shashikanth, Nitesh

AU - Gomez, Guillermo A

AU - Yap, Alpha S

AU - Gottardi, Cara J

AU - de Rooij, Johan

AU - Wang, Ning

AU - Leckband, Deborah E

PY - 2014/4/15

Y1 - 2014/4/15

N2 - 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.

AB - 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.

KW - Actins

KW - Animals

KW - Binding Sites

KW - Biomechanical Phenomena

KW - Cadherins

KW - Cell Adhesion

KW - Cell Line, Tumor

KW - Dogs

KW - Erythrocytes

KW - Humans

KW - Kinetics

KW - Madin Darby Canine Kidney Cells

KW - Mechanotransduction, Cellular

KW - Protein Interaction Domains and Motifs

KW - Protein Transport

KW - Vinculin

KW - alpha Catenin

U2 - 10.1242/jcs.139014

DO - 10.1242/jcs.139014

M3 - Article

C2 - 24522187

SN - 0021-9533

VL - 127

SP - 1779

EP - 1791

JO - Journal of Cell Science

JF - Journal of Cell Science

IS - Pt 8

ER -