Document Detail


An autoinhibited structure of α-catenin and its implications for vinculin recruitment to adherens junctions.
MedLine Citation:
PMID:  23589308     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
α-Catenin is an actin- and vinculin-binding protein that regulates cell-cell adhesion by interacting with cadherin adhesion receptors through β-catenin, but the mechanisms by which it anchors the cadherin-catenin complex to the actin cytoskeleton at adherens junctions remain unclear. Here we determined crystal structures of αE-catenin in the autoinhibited state and the actin-binding domain of αN-catenin. Together with the small-angle x-ray scattering analysis of full-length αN-catenin, we deduced an elongated multidomain assembly of monomeric α-catenin that structurally and functionally couples the vinculin- and actin-binding mechanisms. Cellular and biochemical studies of αE- and αN-catenins show that αE-catenin recruits vinculin to adherens junctions more effectively than αN-catenin, partly because of its higher affinity for actin filaments. We propose a molecular switch mechanism involving multistate conformational changes of α-catenin. This would be driven by actomyosin-generated tension to dynamically regulate the vinculin-assisted linkage between adherens junctions and the actin cytoskeleton.
Authors:
Noboru Ishiyama; Nobutoshi Tanaka; Kentaro Abe; Yoo Jeong Yang; Yazan M Abbas; Masataka Umitsu; Bhushan Nagar; Stephanie A Bueler; John L Rubinstein; Masatoshi Takeichi; Mitsuhiko Ikura
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2013-04-15
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  288     ISSN:  1083-351X     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  2013 May 
Date Detail:
Created Date:  2013-06-04     Completed Date:  2013-08-06     Revised Date:  2014-06-03    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  United States    
Other Details:
Languages:  eng     Pagination:  15913-25     Citation Subset:  IM    
Data Bank Information
Bank Name/Acc. No.:
PDB/4K1N;  4K1O
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MeSH Terms
Descriptor/Qualifier:
Actin Cytoskeleton* / chemistry,  genetics,  metabolism
Adherens Junctions* / chemistry,  genetics,  metabolism
Animals
Cell Line
Crystallography, X-Ray
Mice
Models, Biological*
Nerve Tissue Proteins* / chemistry,  genetics,  metabolism
Protein Structure, Tertiary
Structure-Activity Relationship
Vinculin* / chemistry,  genetics,  metabolism
alpha Catenin* / chemistry,  genetics,  metabolism
Grant Support
ID/Acronym/Agency:
//Canadian Institutes of Health Research
Chemical
Reg. No./Substance:
0/Catna1 protein, mouse; 0/Ctnna2 protein, mouse; 0/Nerve Tissue Proteins; 0/alpha Catenin; 125361-02-6/Vinculin
Comments/Corrections

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