6WVT

Structural basis of alphaE-catenin - F-actin catch bond behavior

Summary for 6WVT

• Entry DOI: 10.2210/pdb6wvt/pdb
• EMDB information: 21925
• Descriptor: Actin, alpha skeletal muscle, Catenin alpha-1, MAGNESIUM ION, ... (4 entities in total)
• Functional Keywords: alphae-catenin, catch bond, adherens junction, cell adhesion
• Biological source: Mus musculus (Mouse); More
• Total number of polymer chains: 12
• Total formula weight: 411364.56

Authors

Xu, X.P.,Pokutta, S.,Torres, M.,Swift, M.F.,Hanein, D.,Volkmann, N.,Weis, W.I. (deposition date: 2020-05-06, release date: 2020-10-07, Last modification date: 2025-04-02)

Primary citation

Xu, X.P.,Pokutta, S.,Torres, M.,Swift, M.F.,Hanein, D.,Volkmann, N.,Weis, W.I.
Structural basis of alpha E-catenin-F-actin catch bond behavior.
Elife, 9:-, 2020

PubMed Abstract: Cell-cell and cell-matrix junctions transmit mechanical forces during tissue morphogenesis and homeostasis. α-Catenin links cell-cell adhesion complexes to the actin cytoskeleton, and mechanical load strengthens its binding to F-actin in a direction-sensitive manner. Specifically, optical trap experiments revealed that force promotes a transition between weak and strong actin-bound states. Here, we describe the cryo-electron microscopy structure of the F-actin-bound αE-catenin actin-binding domain, which in solution forms a five-helix bundle. In the actin-bound structure, the first helix of the bundle dissociates and the remaining four helices and connecting loops rearrange to form the interface with actin. Deletion of the first helix produces strong actin binding in the absence of force, suggesting that the actin-bound structure corresponds to the strong state. Our analysis explains how mechanical force applied to αE-catenin or its homolog vinculin favors the strongly bound state, and the dependence of catch bond strength on the direction of applied force.

PubMed: 32915141
DOI: 10.7554/eLife.60878

Experimental method

ELECTRON MICROSCOPY (3.56 Å)