Association of the protein tyrosine phosphatase PTP1C with the protein tyrosine kinase c‐Src in human platelets

FEBS Letters

Fischer, Siegmund²  Falet, Hervé¹  Bachelot, Christilla¹  Ramos-Morales, Francisco²  Rendu, Francine¹ 

[1] INSERM U 428, UFR des Sciences Pharmaceutiques et Biologiques, Université René Descartes, 4, avenue de l'Observatoire, 75270 Paris Cedex 06, France;INSERM U 363, Institut Cochin de Génétique Moléculaire, 27, rue du Faubourg Saint Jacques, 75014 Paris, France

关键词: Protein tyrosine phosphatase 1C;    c-Src;    SH2 domain;    Human platelet;    PTK;    protein tyrosine kinase;    SH2 domain;    Src homology 2 domain;    PTP;    protein tyrosine phosphatase;    GST;    glutathione S-transferase;    SDS-PAGE;    SDS-polyacrylamide gel electrophoresis;    pTyr;    phosphotyrosine;    NP-40;    Nonidet P-40;   

DOI  :  10.1016/0014-5793(96)00232-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Protein tyrosine phosphatase 1C (PTP1C), highly expressed in hematopoietic cells, is a soluble protein tyrosine phosphatase containing two Src homology 2 (SH2) domains at the N-terminus and two putative sites of tyrosine phosphorylation at the C-terminus. This paper reports that PTP1C and c-Src could be coimmunoprecipitated during thrombin-induced platelet activation. Moreover, association between the two signalling proteins occurred only after PTP1C had been tyrosine phosphorylated. In in vitro experiments, PTP1C bound to the SH2 domain of c-Src, suggesting that association between tyrosine phosphorylated PTP1C and c-Src was mediated by the SH2 domain of c-Src. Finally, in resting platelets, PTP1C was mainly found in the Nonidet P-40 soluble fraction whereas following thrombin-induced activation, around 17% of PTP1C was associated with the insoluble fraction.

【 授权许可】

Unknown