Tyrosine phosphorylation and translocation of LAT in platelets

FEBS Letters

Sarkar, Sibaji¹ 

[1] Department of Pathology and Laboratory Medicine, CB# 7525, Brinkhouse-Bullitt Bldg., Room 605, University of North Carolina, Chapel Hill, NC 27599-7525, USA

关键词: LAT;    Platelet;    Phosphorylation;    Signaling;    TCR;    T-cell receptor;    EGTA;    ethylene glycol-bis(β-amino ethyl ether)-N;    N;    N′;    N′- tetraacetic acid;    PMSF;    phenylmethylsulfonyl fluoride;    PI3kinase;    phosphoinositide 3-kinase;    SDS-PAGE;    sodium dodecyl sulfate polyacrylamide gel electrophoresis;    CONA;    concanavalin A;    FBS;    fetal bovine serum;    PBS;    phosphate-buffered saline;    TBST;    Tris-buffered saline Tween;    RIPA;    radioimmunoprecipitation assay buffer;    HRP;    horseradish peroxidase;    TSF;    Triton-soluble fraction;    RSF;    RIPA-soluble fraction;   

DOI  :  10.1016/S0014-5793(98)01584-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Platelet aggregation is accompanied by the tyrosine phosphorylation of several proteins including syk. However, some of these proteins are not identified. Recent studies showed that LAT is a syk substrate and is tyrosine phosphorylated during T cell stimulation. In this study, we demonstrated that LAT is present in platelets and is tyrosine phosphorylated in response to ADP- and thrombin-stimulated aggregation. Moreover, LAT, like syk and β₃, translocates to the cytoskeleton during the late stage of thrombin-stimulated irreversible aggregation and not during ADP-stimulated reversible aggregation.

【 授权许可】

Unknown