Integrin cytoplasmic domain-binding proteins
Author(s) -
Shouchun Liu,
David Calderwood,
Mark H. Ginsberg
Publication year - 2000
Publication title -
journal of cell science
Language(s) - Uncategorized
Resource type - Journals
SCImago Journal Rank - 2.384
H-Index - 278
eISSN - 1477-9137
pISSN - 0021-9533
DOI - 10.1242/jcs.113.20.3563
Subject(s) - integrin , biology , microbiology and biotechnology , cytoplasm , integrin, beta 6 , filamin , actin cytoskeleton , signal transduction , cytoskeleton , cell adhesion , cd49c , integrin alpha m , receptor , cell , biochemistry
Integrins are a large family of cell surface receptors that mediate cell adhesion and influence migration, signal transduction, and gene expression. The cytoplasmic domains of integrins play a pivotal role in these integrin-mediated cellular functions. Through interaction with the cytoskeleton, signaling molecules, and other cellular proteins, integrin cytoplasmic domains transduce signals from both the outside and inside of the cell and regulate integrin-mediated biological functions. Identification and functional analyses of integrin cytoplasmic domain-binding proteins have been pursued intensively. In recent years, more cellular proteins have been reported to directly interact with integrin cytoplasmic domains and some of these interactions may play important roles in integrin-mediated biological responses. Integrin (&bgr;) chains, for example, interact with actin-binding proteins (e.g. talin and filamin), which form mechanical links to the cytoskeleton. These and other proteins (e.g. FAK, ILK and novel proteins such as TAP20) might also link integrins to signaling mechanisms and, in some cases (e.g. JAB1) mediate integrin-dependent gene regulation.
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