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J Biol Chem, Vol. 274, Issue 46, 32835-32841, November 12, 1999
From INSERM U326, IFR 30, Hopital Purpan,
31059 Toulouse, France, § Max Planck Research Unit,
Molecular Cell Biology, University of Jena, 07747 Jena, Germany, and
¶ CNRS UPR 1086, CRBM, 34293 Montpellier, France
Phosphoinositide 3-kinase (PI3K) has been shown
to play an essential role in G protein-induced signaling even in
non-myeloid cells where few agonists of G protein-coupled receptors are
known to activate PI3K. We have identified adherent cell lines where lysophosphatidic acid (LPA) strongly and rapidly activates the accumulation of PI3K lipid products. The process is not modified by
expression of a kinase-dead mutant of the G
-responsive PI3K p110. In contrast, it is inhibited by genistein or expression of a
dominant negative mutant of p85 and potentiated by overexpressing wild-type p110
or - but not -. By using a specific chemical inhibitor of the epidermal growth factor receptor (EGFR) and expression of a dominant negative mutant, we have observed that recruitment of
p85/p110 PI3Ks occurs through transactivation of the EGFR by LPA and
downstream mobilization of the docking protein Gab1 that associates
with p85 upon LPA stimulation. Finally, we show that LPA cannot
activate PI3K in cell lines lacking the EGFR/Gab1 pathway, including
cells that transactivate the PDGF receptor. Altogether, these results
demonstrate that activation of PI3K by LPA is conditioned by the
ability of LPA to transactivate an EGFR/Gab1 signaling pathway.
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