Focal adhesion kinase and Src mediate integrin regulation of insulin receptor phosphorylation

FEBS Letters

Gautier, Nadine¹  Baron, Véronique¹  El Annabi, Slim¹ 

[1]Institut National de la Santé et de la Recherche Médicale, U145/IFR 50, Faculté de Médecine, Avenue de Valombrose, 06107 Nice Cedex 02, France

关键词: Insulin receptor;    Integrin;    Src kinase;    Focal adhesion kinase;    Adhesion;    FAK;    focal adhesion kinase;    IR;    insulin receptor;    IRS;    insulin receptor substrate;    CHO;    Chinese hamster ovary;    PI3-kinase;    phosphatidyl inositol 3-kinase;    PDGF;    platelet derived growth factor;    EGF;    epidermal growth factor;   

DOI  :  10.1016/S0014-5793(01)02981-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

We show here that phosphorylation of the insulin receptor and insulin receptor substrate-1 is increased when suspended cells are replated on fibronectin. This is not due to decreased numbers of cell surface receptors, alteration of insulin binding, or stimulation of a phosphatase activity in non-adherent cells. Expression of Src together with focal adhesion kinase (FAK) in suspended cells restores insulin-induced receptor autophosphorylation to levels observed in fibronectin-attached cells. Conversely, expression of dominant-negative mutants of either Src or FAK abolishes potentiation of insulin receptor phosphorylation by cell adhesion. The results suggest that both Src and FAK participate in integrin-mediated regulation of insulin receptor signal.

【 授权许可】

Unknown