Translocation of an SH2‐containing protein tyrosine phosphatase (SH‐PTP1) to the cytoskeleton of thrombin‐activated platelets

FEBS Letters

Ragab, Ashraf¹  Chap, Hugues¹  Li, Ruo Ya¹  Ragab-Thomas, Jeannie M.F.¹  Gaits, Frédérique¹ 

[1] INSERM Unité 326, Phospholipides Membranaires, Signalisation Cellulaire et Lipoprotéines, Université Paul Sabotier, Hôpital Purpan, 31059 Toulouse Cedex, France

关键词: Platelet;    Thrombin;    Protein tyrosine phosphatase;    Cytoskeleton;    SH2;    PTK;    protein tyrosine kinase;    PTP;    protein tyrosine phosphatase;    PI;    phosphatidylinositol;   

DOI  :  10.1016/0014-5793(94)80613-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A significant protein tyrosine phosphatase (PTP) activity was found to be associated with the cytoskeleton of thrombin-stimulated platelets. Translocation of the enzyme became maximal within 1-2 min of thrombin stimulation and was suppressed by cytochalasin D or upon inhibition of aggregation. Immunoblotting as well as immunoprecipitation revealed that a PTP with two SH2 domains (SH-PTP1) displayed the same behaviour, translocation to the cytoskeleton showing the same time course as that observed for pp60 ^c-src . We conclude that SH-PTP1 might represent a critical enzyme in the complex interplay between the various proteins regulating protein tyrosine phosphorylation in the cytoskeletal matrix.

【 授权许可】

Unknown