Crystal structure of the M-fragment of alpha-catenin: implications for modulation of cell adhesion

Yang, J., Dokurno, P., Tonks, N. K., Barford, D. (2001) Crystal structure of the M-fragment of alpha-catenin: implications for modulation of cell adhesion. Embo Journal, 20 (14). pp. 3645-3656. ISSN 0261-4189

URL: http://www.ncbi.nlm.nih.gov/pubmed/11447106
DOI: 10.1093/emboj/20.14.3645

Abstract

The cytoskeletal protein alpha -catenin, which shares structural similarity with vinculin, is required for cadherin-mediated cell adhesion, and functions to modulate cell adhesive strength and to link the cadherins to the actin-based cytoskeleton. Here we describe the crystal structure of a region of alpha -catenin (residues 377-633) termed the M-fragment. The M-fragment is composed of a tandem repeat of two antiparallel four-helix bundles of virtually identical architectures that are related in structure to the dimerization domain of (alpha -catenin and the tail region of vinculin. These results suggest that (alpha -catenin is composed of repeating antiparallel helical domains. The region of (alpha -catenin previously defined as an adhesion modulation domain corresponds to the C-terminal four-helix bundle of the M-fragment, and in the crystal lattice these domains exist as dimers. Evidence for dimerization of the M-fragment of alpha -catenin in solution was detected by chemical crosslinking experiments. The tendency of the adhesion modulation domain to form dimers may explain its biological activity of promoting cell-cell adhesiveness by inducing lateral dimerization of the associated cadherin molecule.

Item Type: Paper
Uncontrolled Keywords: cadherins alpha-catenin cell adhesion protein structure X-ray crystallography SECONDARY STRUCTURE PREDICTION CADHERIN CYTOPLASMIC DOMAIN PROSTATE-CANCER CELLS BETA-CATENIN FUNCTIONAL-ANALYSIS ADHERENS JUNCTIONS COMPLEX-FORMATION EPITHELIAL-CELLS PROTEIN VINCULIN
Subjects: bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > catenins
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > cytoskeletal proteins
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types
Investigative techniques and equipment > x ray crystallography
CSHL Authors:
Communities: CSHL labs > Tonks lab
Depositing User: Matt Covey
Date Deposited: 18 Dec 2013 19:29
Last Modified: 18 Dec 2013 19:29
PMCID: PMC125534
Related URLs:
URI: http://repository.cshl.edu/id/eprint/29013

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