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

被引：35

作者：

Falet, H ^{[1
]}

RamosMorales, F ^{[1
]}

Bachelot, C ^{[1
]}

Fischer, S ^{[1
]}

Rendu, F ^{[1
]}

机构：

[1] INST COCHIN GENET MOLEC, INSERM, U363, F-75014 PARIS, FRANCE

来源：

FEBS LETTERS | 1996年 / 383卷 / 03期

关键词：

protein tyrosine phosphatase 1C; c-Src; SH2; domain; human platelet;

D O I：

10.1016/0014-5793(96)00232-3

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

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.

引用

页码：165 / 169

页数：5

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