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Crystal structure of the M‐fragment of α‐catenin: implications for modulation of cell adhesion
Author(s) -
Yang Jing,
Dokurno Pawel,
Tonks Nicholas K.,
Barford David
Publication year - 2001
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1093/emboj/20.14.3645
Subject(s) - biology , fragment (logic) , alpha (finance) , adhesion , cell adhesion , microbiology and biotechnology , biophysics , cell , genetics , materials science , composite material , medicine , construct validity , nursing , computer science , patient satisfaction , programming language
The cytoskeletal protein α‐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 α‐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 α‐catenin and the tail region of vinculin. These results suggest that α‐catenin is composed of repeating antiparallel helical domains. The region of α‐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 α‐catenin in solution was detected by chemical cross‐linking 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.