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J Biol Chem, Vol. 273, Issue 12, 7038-7043, March 20, 1998
From the Afdeling Biochemie, Faculteit Geneeskunde, Campus
Gasthuisberg, Katholieke Universiteit Leuven, Herestraat,
B-3000 Leuven, Belgium
Platelet-derived growth factor (PDGF)
stimulates protein kinase D (PKD) in a time- and
dose-dependent manner. We have used a series of PDGF
receptor mutants that display a selective impairment of the binding of
SH2-containing proteins (GTPase-activating protein, SHP-2,
phospholipase C
Platelet-derived Growth Factor Stimulates Protein Kinase D
through the Activation of Phospholipase C
and Protein Kinase C
(PLC), or phosphatidylinositol 3'-kinase (PI3K))
to show that Tyr-1021, the PLC-binding site, is essential for PKD
stimulation by PDGF in A431 cells. We next investigated whether any one
of these four binding sites could mediate PKD activation in the absence
of the other three sites. F5, a receptor mutant that lacks all four
binding sites for GTPase-activating protein, PLC, PI3K, and SHP-2,
fails to activate PKD. A panel of single add-back mutants was used to
investigate if any one of these four sites could restore signaling to
PKD. Of the four sites, only the PLC+ single
add-back receptor restored PDGF-mediated activation of PKD, and only
this add-back receptor produced diacylglycerol (DAG) in a
PDGF-dependent manner.
1,2-Dioctanoyl-sn-glycerol, a membrane-permeant DAG analog,
was found to be sufficient for activation of PKD. Taken together, these
data indicate that PLC activation is not only necessary, but also
sufficient to mediate PDGF-induced PKD activation. Although the
presence of a pleckstrin homology domain makes PKD a potential PI3K
target, PKD was not stimulated by selective PI3K activation, and
wortmannin, an inhibitor of PI3K, did not inhibit PDGF signaling to
PKD. The activation of PKD by DAG or by the wild-type and
PLC+ add-back PDGF receptors was inhibited by GF109203X,
suggesting a role for protein kinase C in the stimulation of PKD by
PDGF. PDGF induced a time-dependent phosphorylation of PKD
that closely correlated with activation. The PDGF-induced activation
and phosphorylation of PKD were reversed by in vitro
incubation of PKD with protein phosphatase 1 or 2A, indicating
that PDGF signaling to PKD involves the Ser/Thr phosphorylation of PKD.
Taken together, these results conclusively show that PDGF activates PKD
through a pathway that involves activation of PLC and, subsequently,
protein kinase C.
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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