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Focal adhesion kinase and Src mediate integrin regulation of insulin receptor phosphorylation
Author(s) -
El Annabi Slim,
Gautier Nadine,
Baron Véronique
Publication year - 2001
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(01)02981-7
Subject(s) - insulin receptor , autophosphorylation , focal adhesion , insulin receptor substrate , microbiology and biotechnology , proto oncogene tyrosine protein kinase src , fibronectin , irs2 , insulin like growth factor 1 receptor , phosphorylation , biology , integrin , chemistry , receptor , insulin , endocrinology , protein kinase a , biochemistry , insulin resistance , extracellular matrix , growth factor
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.