Phosphatidylinositol 4,5‐bisphosphate specifically stimulates PP60c‐src catalyzed phosphorylation of gelsolin and related actin‐binding proteins

FEBS Letters

De Corte, Veerle¹  Vandekerckhove, Joël¹  Gettemans, Jan¹ 

[1] Flanders Interuniversity Institute of Biotechnology, Department of Biochemistry, Faculty of Medicine, Universiteit Gent, Ledeganckstraat 35, B-9000 Gent, Belgium

关键词: Gelsolin;    Phosphorylation;    pp60c-src;    Protein kinase C;    Phosphatidylinositol 4;    5-bisphosphate;    Cer;    ceramide;    DTT;    dithiothreitol;    PA;    phosphatidic acid;    PC;    phosphatidylcholine;    PE;    phosphatidylethanolamine;    PI;    phosphatidylinositol;    PI-3 kinase;    phosphatidylinositol-3 kinase;    PIP;    phosphatidylinositol 4-monophosphate;    PIP2;    phosphatidylinositol 4;    5-bisphosphate;    PKC;    protein kinase C;    PS;    phosphatidylserine;    SDS-PAGE;    sodium dodecyl sulfate-polyacrylamide gel electrophoresis;    TFA;    trifluoroacetic acid;   

DOI  :  10.1016/S0014-5793(96)01471-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Gelsolin is a widely distributed Ca²⁺-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 (PIP₂), 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 PIP₂-stimulated pp60^c-src phosphorylation.

【 授权许可】

Unknown