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Vinculin and α‐catenin: shared and unique functions in adherens junctions
Author(s) -
Rüdiger Manfred
Publication year - 1998
Publication title -
bioessays
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.175
H-Index - 184
eISSN - 1521-1878
pISSN - 0265-9247
DOI - 10.1002/(sici)1521-1878(199809)20:9<733::aid-bies6>3.0.co;2-h
Subject(s) - adherens junction , vinculin , catenin , microbiology and biotechnology , biology , cadherin , genetics , wnt signaling pathway , signal transduction , cell , focal adhesion
Vinculin and α‐catenin are two functionally related proteins of adherens junctions, structures in which cells make contacts to neighboring cells or to the extracellular matrix. At these sites, the actin cytoskeleton of animal cells is anchored to the plasma membrane. Junction assembly and disassembly are coordinated in processes as different as mitosis, cell movement and tissue formation. Since adherens junctions are assembled from a large number of proteins, these molecules have to be coordinately activated and spatially regulated. Vinculin and α‐catenin have been characterized as tumor suppressors, suggesting that they have a regulatory function in addition to their structural role. Several possible modes of vinculin and α‐catenin regulation are discussed here, as the published data favor the concept that no single model fully explains the complexity of adherens junctions. Most probably, cells select from a variety of possibilities to solve the problem of making specific contacts. BioEssays 20 :733–740, 1998.© 1998 John Wiley and Sons, Inc.