APS, an adapter protein with a PH and SH2 domain, is a substrate for the insulin receptor kinase

被引：49

作者：

Ahmed, Z

Smith, BJ

Kotani, K

Wilden, P

Pillay, TS ^{[1
]}

机构：

[1] Univ Nottingham, Sch Med, Queens Med Ctr, Mol Endocrinol Grp,Inst Cell Signalling, Nottingham NG7 2UH, England

[2] Univ Nottingham, Sch Med, Queens Med Ctr, Sch Biomed Sci, Nottingham NG7 2UH, England

[3] Univ London Imperial Coll Sci Technol & Med, Cell Signalling Lab, Dept Metab Med, London W12 0NN, England

[4] Univ Missouri, Dept Pharmacol, Sch Med, Columbia, MO 65212 USA

[5] Univ Missouri, Program Mol Biol, Sch Med, Columbia, MO 65212 USA

来源：

BIOCHEMICAL JOURNAL | 1999年 / 341卷

基金：

英国惠康基金;

关键词：

tyrosine kinase; tyrosine phosphorylation; yeast two-hybrid system;

D O I：

10.1042/0264-6021:3410665

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：

APS (adapter protein with a PH and SH2 domain) is the newest member of a family of tyrosine kinase adapter proteins including SH2-B and Lnk. We previously identified SH2-B as an insulin-receptor-binding protein and substrate [Kotani, Wilden and Pillay (1998) Biochem J. 335, 103-109]. Here we show that APS interacts with the insulin receptor kinase activation loop through its SH2 domain and insulin stimulates the tyrosine-phosphorylation of APS. Furthermore, the phosphorylation activation-loop tyrosine residues 1158 and 1162 are required for this interaction.

引用

页码：665 / 668

页数：4

共 33 条

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