期刊
NATURE STRUCTURAL & MOLECULAR BIOLOGY
卷 20, 期 2, 页码 188-193出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb.2479
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资金
- US National Institute of General Medical Sciences from the US National Institutes of Health [GM071596, GM094483]
- State of Florida
The F-actin-binding cytoskeletal protein a-catenin interacts with beta-catenin-cadherin complexes and stabilizes cell-cell junctions. The beta-catenin-alpha-catenin complex cannot bind F-actin, whereas interactions of alpha-catenin with the cytoskeletal protein vinculin appear to be necessary to stabilize adherens junctions. Here we report the crystal structure of nearly full-length human alpha-catenin at 3.7-angstrom resolution. alpha-catenin forms an asymmetric dimer where the four-helix bundle domains of each subunit engage in distinct intermolecular interactions. This results in a left handshake-like dimer, wherein the two subunits have remarkably different conformations. The crystal structure explains why dimeric alpha-catenin has a higher affinity for F-actin than does monomeric alpha-catenin, why the beta-catenin-alpha-catenin complex does not bind F-actin, how activated vinculin links the cadherin-catenin complex to the cytoskeleton and why a-catenin but not inactive vinculin can bind F-actin.
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