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Phosphatidylinositol 4,5‐bisphosphate specifically stimulates PP60 c‐src catalyzed phosphorylation of gelsolin and related actin‐binding proteins
Author(s) -
De Corte Veerle,
Gettemans Jan,
Vandekerckhove Joël
Publication year - 1997
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/s0014-5793(96)01471-8
Subject(s) - gelsolin , phosphorylation , phosphatidylinositol , phosphatidylinositol 4,5 bisphosphate , actin , microbiology and biotechnology , profilin , kinase , tyrosine phosphorylation , actin binding protein , biology , chemistry , biochemistry , actin cytoskeleton , cytoskeleton , cell
Gelsolin is a widely distributed Ca 2+ ‐dependent regulator of the cortical actin network. We demonstrate that gelsolin is phosphorylated by pp60 c‐src and that this phosphorylation is dramatically enhanced by phosphatidylinositol 4,5‐bisphosphate (PIP 2 ), known to specifically interact with gelsolin. Other phospholipids display only a marginal effect. pp56 lck , a tyrosine kinase of the same family, does not phosphorylate gelsolin. Other mammalian actin‐binding proteins such as profilin and CapG but also fragmin from Physarum polycephalum are similar targets for PIP 2 ‐stimulated pp60 c‐src phosphorylation.