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(Received for publication, May 2, 1996, and in revised form, August 12, 1996)
From the Cancer Biology Laboratories, Department of Pathology,
College of Veterinary Medicine, Cornell University,
Ithaca, New York 14853
We have shown previously that cell adhesion or
platelet-derived growth factor (PDGF) promotes the in vivo
association of focal adhesion kinase (FAK) with phosphatidylinositol
(PI) 3-kinase. In vitro experiments indicated that this
interaction was mediated by the p85 subunit of PI 3-kinase and
dependent on the tyrosine phosphorylation of FAK. Here we report data
suggesting that the major autophosphorylation site of FAK (Tyr-397) is
the binding site for the SH2 domains of p85 in vitro and is
also required for the association of FAK with PI 3-kinase in
vivo. We also show that Tyr-397 is responsible for the increased
FAK:PI 3-kinase association upon PDGF stimulation, implying that no
additional site of FAK was involved in its binding to PI 3-kinase after
PDGF stimulation. Finally, we present evidence that the interaction of
PI 3-kinase with Tyr-397 of FAK stimulates its activity. Together,
these results suggest that FAK activation and autophosphorylation at
Tyr-397 may lead to its association with PI 3-kinase through the SH2
domains of p85, which can subsequently activate PI 3-kinase during cell
adhesion.
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