Thrombin‐induced association of SHP‐2 with multiple tyrosine‐phosphorylated proteins in human platelets

FEBS Letters

Crosby, D.A¹  Edmead, C.E¹  Poole, A.W¹  Southcott, M¹ 

[1] Department of Pharmacology, School of Medical Sciences, University of Bristol, University Walk, Bristol BS8 1TD, UK

关键词: SH2 domain containing phosphatase-2;    Platelet endothelial cell adhesion molecule-1;    Platelet;    Tyrosine phosphatase;    SHP-2;    SH2 domain containing phosphatase-2;    PECAM-1;    platelet endothelial cell adhesion molecule-1;    WGA;    wheat germ agglutinin;   

DOI  :  10.1016/S0014-5793(99)01209-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

SH2 domain containing phosphatase-2 (SHP-2) has an important regulatory role in a variety of cell types. However, little is known concerning its function in platelets. We show here that, in thrombin-stimulated human platelets, SHP-2 undergoes a time-dependent association with platelet endothelial cell adhesion molecule-1 (PECAM-1) and four low molecular weight phosphoproteins which are attenuated by the Src kinase inhibitor PP1. The low molecular weight proteins, which may be transmembrane proteins, are shown to bind exclusively to the N-terminal SH2 domain of SHP-2 and are therefore possible activators of the phosphatase. In addition, SHP-2 phosphatase activity is shown to be increased following thrombin stimulation or cross-linking of PECAM.

【 授权许可】

Unknown