Binding of SH2 containing proteins to the insulin receptor: A new way for modulating insulin signalling

被引：28

作者：

Liu, F

Roth, RA ^{[1
]}

机构：

[1] Stanford Univ, Sch Med, Dept Mol Pharmacol, Stanford, CA 94305 USA

[2] Univ Texas, Hlth Sci Ctr, Dept Pharmacol, San Antonio, TX 78284 USA

来源：

MOLECULAR AND CELLULAR BIOCHEMISTRY | 1998年 / 182卷 / 1-2期

关键词：

SH2; domains; insulin receptor; tyrosine phosphorylation;

D O I：

10.1023/A:1006899832614

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

Prior studies have established a role in insulin action for the tyrosine phosphorylation of substrates and their subsequent complexing with SH2 containing proteins. More recently, SH2 proteins have been identified which can tightly bind to the tyrosine phosphorylated insulin receptor. The major protein identified so far (called Grb-IR or Grb10) of this type appears to be present in at least 3 isoforms, varying in the presence of a pleckstrin homology domain and in the sequence of its amino terminus. The binding of this protein to the insulin receptor appears to inhibit signalling by the receptor. The present review will discuss the current knowledge of the structure and function of this protein.

引用

页码：73 / 78

页数：6

共 43 条

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