The α‐isoform of class II phosphoinositide 3‐kinase is more effectively activated by insulin receptors than IGF receptors, and activation requires receptor NPEY motifs

FEBS Letters

Shepherd, P.R.²  Siddle, K.¹  Ursø, B.¹  O'Rahilly, S.¹  Brown, R.A.² 

[1] University of Cambridge, Department of Clinical Biochemistry, Addenbrooke's Hospital, Cambridge CB2 2QR, UK;Department of Biochemistry and Molecular Biology, University College London, Gower Street, London WC1E 6BT, UK

关键词: Insulin;    Insulin-like growth factor;    Receptor;    Phosphoinositide 3-kinase;    C2α;    3T3-L1 adipocyte;    IGF;    insulin-like growth factor;    IR;    insulin receptor;    IGFR;    type I IGF receptor;    TIR;    TrkC-insulin receptor chimaera;    TIGR;    TrkC-IGF receptor chimaera;    IRS;    insulin receptor substrate;    PI3K;    phosphoinositide 3-kinase;    PTB;    phosphotyrosine binding;    NT-3;    neurotrophin-3;    PBS;    phosphate-buffered saline;   

DOI  :  10.1016/S0014-5793(99)01388-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Little is known about the physiological role and mechanism of activation of class II phosphoinositide 3-kinases (PI3Ks), although it has been shown that the PI3K-C2α isoform is activated by insulin. Using chimaeric receptor constructs which can be activated independently of endogenous receptors in transfected cells, we found that PI3K-C2α activity was stimulated to a greater extent by insulin receptors than IGF receptors in 3T3-L1 adipocytes. Activation of PI3K-C2α required an intact NPEY motif in the receptor juxtamembrane domain. We conclude that PI3K-C2α is a candidate for participation in insulin-specific intracellular signalling.

【 授权许可】

Unknown