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.
Original language | English |
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Pages (from-to) | 1779-91 |
Number of pages | 13 |
Journal | Journal of Cell Science |
Volume | 127 |
Issue number | Pt 8 |
DOIs | |
Publication status | Published - 15 Apr 2014 |
Keywords
- Actins
- Animals
- Binding Sites
- Biomechanical Phenomena
- Cadherins
- Cell Adhesion
- Cell Line, Tumor
- Dogs
- Erythrocytes
- Humans
- Kinetics
- Madin Darby Canine Kidney Cells
- Mechanotransduction, Cellular
- Protein Interaction Domains and Motifs
- Protein Transport
- Vinculin
- alpha Catenin