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Vinculin and metavinculin: Oligomerization and interactions with F‐actin
Author(s) -
Thompson Peter M.,
Tolbert Caitlin E.,
Campbell Sharon L.
Publication year - 2013
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2013.02.042
Subject(s) - vinculin , actin , microbiology and biotechnology , focal adhesion , cytoskeleton , cell adhesion , function (biology) , actin cytoskeleton , chemistry , adhesion , biophysics , biology , biochemistry , cell , signal transduction , organic chemistry
Vinculin, and its splice variant metavinculin, are scaffolding proteins that localize to cellular adhesions. Vinculin is a key player in mediating cell adhesion, motility, and cellular response to force. In the past decade, a number of new studies have evaluated the importance of vinculin oligomers, especially in their role of bundling F‐actin. Emerging evidence also suggests that vinculin oligomerization is important for vinculin's scaffolding function. Here we describe the latest findings on vinculin's interaction with F‐actin and we clarify the different known vinculin oligomers. Differences in these functions between vinculin and metavinculin provide key insights to the structure and function of these oligomers, and should guide further studies.