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PHOSPHORYLATION OF FILAMIN (ABP‐280) REGULATES THE BINDING TO THE LIPID MEMBRANE, INTEGRIN, AND ACTIN
Author(s) -
Goldmann Wolfgang H.
Publication year - 2001
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 - 10.1006/cbir.2000.0710
Subject(s) - filamin , phosphoprotein , microbiology and biotechnology , actin binding protein , phosphorylation , actin , cytoplasm , glycoprotein , tyrosine phosphorylation , lipid raft , chemistry , cell surface receptor , actin cytoskeleton , receptor , biology , cytoskeleton , cell , biochemistry , signal transduction
Actin‐binding protein (ABP‐280; filamin) is a phosphoprotein present in the periphery of the cytoplasm, where it can cross‐link actin filaments, associate with lipid membranes, and bind to membrane surface receptors. Given its function and localization in the cell, the hypothesis that it serves as a substrate for p56 lck , a lymphocyte‐specific member of the src family of protein tyrosine kinases associated with cell surface glycoproteins is considered. The results suggest conformationally‐induced regulation of filamin (ABP‐280).