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Correlation between the interaction of the vinculin tail domain with lipid membranes, its phosphorylation and cell mechanical behaviour
Author(s) -
Goldmann Wolfgang H.
Publication year - 2010
Publication title -
cell biology international
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.932
H-Index - 77
eISSN - 1095-8355
pISSN - 1065-6995
DOI - 10.1042/cbi20100085
Subject(s) - vinculin , focal adhesion , integrin , cytoskeleton , extracellular matrix , transmembrane protein , microbiology and biotechnology , cell adhesion , chemistry , phosphorylation , adhesion , cell membrane , cell , extracellular , cell surface receptor , membrane , transmembrane domain , biophysics , receptor , biochemistry , biology , organic chemistry
Cell adhesion and cell–cell contacts are a pre‐requisite for proper metabolism, protein synthesis and cell survival. Integrins are the transmembrane receptors that link the extracellular matrix via the FAC (focal adhesion complex) with the cytoskeleton. Vinculin is a pivotal FAC protein that has not only been implicated in regulating FAC formation and transmitting mechanical forces, but also in associating with membranous lipids in biological systems.