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 Lettjournal_title
FEBS lettersauthors
El Annabi S,Gautier N,Baron Vdoi
10.1016/s0014-5793(01)02981-7keywords:
subject
Has Abstractpub_date
2001-11-02 00:00:00pages
247-52issue
3eissn
0014-5793issn
1873-3468pii
S0014-5793(01)02981-7journal_volume
507pub_type
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