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J. Biol. Chem., Vol. 275, Issue 30, 23333-23339, July 28, 2000
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From the Beatson Institute for Cancer Research, Garscube Estate,
Switchback Road, Bearsden, Glasgow, G61 1BD, United Kingdom
The non-receptor tyrosine kinase FAK plays a key
role at sites of cellular adhesion. It is subject to regulatory
tyrosine phosphorylation in response to a variety of stimuli, including integrin engagement after attachment to extracellular matrix, oncogene
activation, and growth factor stimulation. Here we use an antibody that
specifically recognizes the phosphorylated form of the putative FAK
autophosphorylation site, Tyr397. We demonstrate that
FAK phosphorylation induced by integrins during focal adhesion assembly
differs from that induced by activation of a temperature-sensitive
v-Src, which is associated with focal adhesion turnover and
transformation. Specifically, although v-Src induces tyrosine
phosphorylation of FAK, there is no detectable phosphorylation of
Tyr397. Moreover, activation of v-Src results in a net
decrease in fibronectin-stimulated phosphorylation of
Tyr397, suggesting possible antagonism between v-Src and
integrin-induced phosphorylation. Our mutational analysis further
indicates that the binding of v-Src to Tyr397 of FAK in its
phosphorylated form, which is normally mediated, at least in part, by
the SH2 domain of Src, is not essential for v-Src-induced cell
transformation. We conclude that different stimuli can induce
phosphorylation of FAK on distinct tyrosine residues, linking specific
phosphorylation events to ensuing biological responses.
v-Src Induces Tyrosine Phosphorylation of Focal Adhesion
Kinase Independently of Tyrosine 397 and Formation of a Complex
with Src*
,
*
This work was supported by the Cancer Research Campaign.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed. Tel.: 0141-330-3954;
Fax: 0141-942-6521; E-mail: g.mclean@beatson.gla.ac.uk.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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