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J Biol Chem, Vol. 273, Issue 40, 25777-25782, October 2, 1998
§,,
,
From the Focal adhesion kinase (FAK) is a cytoplasmic
tyrosine kinase involved in integrin-mediated signal transduction
pathway. In this report, we describe that the treatment of hepatocyte
growth factor (HGF) stimulates a significant increase in the tyrosine phosphorylation of FAK in human embryonic kidney 293 cells. This stimulation is independent of cell adhesion or the integrity of the
actin cytoskeleton, suggesting potentially different mechanisms by
which the HGF receptors and integrins regulate the tyrosine phosphorylation of FAK. Our results also suggest that the activation of
Src upon HGF stimulation is likely to be one, if not the only, of the
mechanisms responsible for the HGF-induced tyrosine phosphorylation of
FAK. Furthermore, we showed that a mutation in the Grb2 binding site
Tyr-925 of FAK partially abolishes its increase in HGF-induced phosphorylation. Finally, we demonstrated that HGF stimulates the
association of FAK with Grb2 in vitro and in intact cells and provided evidence that FAK might contribute to the activation of
mitogen-activated protein kinase through Ras in HGF signaling by
functioning as an adapter molecule.
Department of Zoology and the
§ Institute of Biochemistry, Department of Veterinary Medicine, Department of Physiology,
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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