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J Biol Chem, Vol. 273, Issue 37, 23750-23757, September 11, 1998
-mediated Calcium Signaling
,
,, and
From the Divisions of It has been demonstrated that the lipid products
of the phosphoinositide 3-kinase (PI3K) can associate with the Src
homology 2 (SH2) domains of specific signaling molecules and modify
their actions. In the current experiments, phosphatidylinositol
3,4,5-trisphosphate (PtdIns-3,4,5-P3) was found to
bind to the C-terminal SH2 domain of phospholipase C Signal Transduction and
¶ Nephrology, Beth Israel Deaconess Medical Center, Harvard
Medical School, Boston, Massachusetts 02215, the Schepens Eye
Research Institute, Boston, Massachusetts 02114, and the
§ Laboratory of Cell Signaling, NHLBI, National Institutes
of Health, Bethesda, Maryland 20892
(PLC) with
an apparent Kd of 2.4 µM and to
displace the C-terminal SH2 domain from the activated platelet-derived
growth factor receptor (PDGFR). To investigate the in vivo
relevance of this observation, intracellular inositol trisphosphate
(IP3) generation and calcium release were examined in HepG2
cells expressing a series of PDGFR mutants that activate PLC with or
without receptor association with PI3K. Coactivation of PLC and PI3K
resulted in an ~40% increase in both intracellular IP3
generation and intracellular calcium release as compared with selective
activation of PLC. Similarly, the addition of wortmannin or LY294002
to cells expressing the wild-type PDGFR inhibited the release of
intracellular calcium. Thus, generation of PtdIns-3,4,5-P3 by receptor-associated PI3K causes an increase in IP3
production and intracellular calcium release, potentially via enhanced
PtdIns-4,5-P2 substrate availability due to
PtdIns-3,4,5-P3-mediated recruitment of PLC to the lipid
bilayer.
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