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

Abstract:

: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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

El Annabi S,Gautier N,Baron V

doi

10.1016/s0014-5793(01)02981-7

keywords:

subject

Has Abstract

pub_date

2001-11-02 00:00:00

pages

247-52

issue

3

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(01)02981-7

journal_volume

507

pub_type

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