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Science. 2014 Oct 31;346(6209):1254211. doi: 10.1126/science.1254211.

Cell adhesion. The minimal cadherin-catenin complex binds to actin filaments under force.

Author information

1
Department of Chemical Engineering, Stanford University, Stanford, CA 94305, USA.
2
Biophysics Program, Stanford University, Stanford, CA 94305, USA.
3
Bioinformatics and Structural Systems Biology Program, Sanford-Burnham Medical Research Institute, La Jolla, CA 92037.
4
Department of Structural Biology, Stanford University, Stanford, CA 94305, USA.
5
Department of Molecular and Cellular Physiology, Stanford University, Stanford, CA 94305, USA.
6
Department of Biology, Stanford University, Stanford, CA 94305, USA.
7
Stanford Cardiovascular Institute, Stanford University, Stanford, CA 94305, USA.
#
Contributed equally

Abstract

Linkage between the adherens junction (AJ) and the actin cytoskeleton is required for tissue development and homeostasis. In vivo findings indicated that the AJ proteins E-cadherin, β-catenin, and the filamentous (F)-actin binding protein αE-catenin form a minimal cadherin-catenin complex that binds directly to F-actin. Biochemical studies challenged this model because the purified cadherin-catenin complex does not bind F-actin in solution. Here, we reconciled this difference. Using an optical trap-based assay, we showed that the minimal cadherin-catenin complex formed stable bonds with an actin filament under force. Bond dissociation kinetics can be explained by a catch-bond model in which force shifts the bond from a weakly to a strongly bound state. These results may explain how the cadherin-catenin complex transduces mechanical forces at cell-cell junctions.

PMID:
25359979
PMCID:
PMC4364042
DOI:
10.1126/science.1254211
[Indexed for MEDLINE]
Free PMC Article

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