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

[1] Site-directed mutagenesis and yeast two-hybrid studies of the insulin and insulin-like growth factor-1 receptors: The Src homology-2 domain-containing protein hGrb10 binds to the autophosphorylated tyrosine residues in the kinase domain of the insulin receptor [J].

Dong, LQ ;

Farris, S ;

Christal, J ;

Liu, F .

MOLECULAR ENDOCRINOLOGY, 1997, 11 (12) :1757-1765

[2] THE HUMAN INSULIN-RECEPTOR CDNA - THE STRUCTURAL BASIS FOR HORMONE-ACTIVATED TRANSMEMBRANE SIGNALING [J].

EBINA, Y ;

ELLIS, L ;

JARNAGIN, K ;

EDERY, M ;

GRAF, L ;

CLAUSER, E ;

OU, JH ;

MASIARZ, F ;

KAN, YW ;

GOLDFINE, ID ;

ROTH, RA ;

RUTTER, WJ .

CELL, 1985, 40 (04) :747-758

[3] Human GRB-IR beta/GRB10 - Splice variants of an insulin and growth factor receptor-binding protein with PH and SH2 domains [J].

Frantz, JD ;

GiorgettiPeraldi, S ;

Ottinger, EA ;

Shoelson, SE .

JOURNAL OF BIOLOGICAL CHEMISTRY, 1997, 272 (05) :2659-2667

[4]

GUSTAFSON TA, 1995, MOL CELL BIOL, V15, P2500

[5] Interaction between the Grb10 SH2 domain and the insulin receptor carboxyl terminus [J].

Hansen, H ;

Svensson, U ;

Zhu, JW ;

Laviola, L ;

Giorgino, F ;

Wolf, G ;

Smith, RJ ;

Riedel, H .

JOURNAL OF BIOLOGICAL CHEMISTRY, 1996, 271 (15) :8882-8886

[6] From receptor to transporter: insulin signalling to glucose transport [J].

Holman, GD ;

Kasuga, M .

DIABETOLOGIA, 1997, 40 (09) :991-1003

[7] CLONING AND CHARACTERIZATION OF LNK, A SIGNAL-TRANSDUCTION PROTEIN THAT LINKS T-CELL RECEPTOR ACTIVATION SIGNAL TO PHOSPHOLIPASE C-GAMMA(1), GRB2, AND PHOSPHATIDYLINOSITOL 3-KINASE [J].

HUANG, XM ;

LI, YJ ;

TANAKA, K ;

MOORE, KG ;

HAYASHI, JI .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1995, 92 (25) :11618-11622

[8] SH2-Bα is an insulin-receptor adapter protein and substrate that interacts with the activation loop of the insulin-receptor kinase [J].

Kotani, K ;

Wilden, P ;

Pillay, TS .

BIOCHEMICAL JOURNAL, 1998, 335 :103-109

[9] The adapter protein Grb10 associates preferentially with the insulin receptor as compared with the IGF-I receptor in mouse fibroblasts [J].

Laviola, L ;

Giorgino, F ;

Chow, JC ;

Baquero, JA ;

Hansen, H ;

Ooi, J ;

Zhu, JW ;

Riedel, H ;

Smith, RJ .

JOURNAL OF CLINICAL INVESTIGATION, 1997, 99 (05) :830-837

[10] Binding of SH2 containing proteins to the insulin receptor: A new way for modulating insulin signalling [J].

Liu, F ;

Roth, RA .

MOLECULAR AND CELLULAR BIOCHEMISTRY, 1998, 182 (1-2) :73-78

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