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J Biol Chem, Vol. 273, Issue 36, 23110-23117, September 4, 1998
From the Division of Signal Transduction, Department of Medicine,
Beth Israel Deaconess Medical Center, Boston, Massachusetts 02215
The activation of growth factor
receptors and receptors coupled to heterotrimeric guanine
nucleotide-binding proteins (G-proteins) can increase mitogen-activated
protein (MAP) kinase activity in many cells. Previously, we
demonstrated that the activation of G-protein-coupled
P2Y2 receptors by extracellular ATP and UTP stimulated MAP (p42 ERK2) kinase by a mechanism that was dependent on
the elevation of [Ca2+]i and the activation of
related adhesion focal tyrosine kinase (RAFTK) (also called PYK2,
CAK
, and CADTK) and protein kinase C (PKC). Here, we examine further
the signaling cascade between the P2Y2 receptor and MAP
kinase. MAP kinase was transiently activated by exposure of PC12 cells
to UTP. UTP, ionomycin, and phorbol ester (phorbol 12-myristate
13-acetate) increased MAP kinase activity and also promoted the
tyrosine phosphorylation of RAFTK, the epidermal growth factor (EGF)
receptor, SHC, and p120cbl. Down-regulation of PKC and
inhibition of the elevation of [Ca2+]i,
conditions that block the activation of MAP kinase, also blocked the
increases in the tyrosine phosphorylation of RAFTK and the EGF
receptor. AG1478, a tyrphostin selective for the EGF receptor, reduced
the activation of MAP kinase, the tyrosine phosphorylation of SHC, the
association of Grb2 with SHC, and the tyrosine phosphorylation of the
EGF receptor and p120cbl but did not block the tyrosine
phosphorylation of RAFTK. The similar effects of UTP, ionomycin, and
phorbol 12-myristate 13-acetate (PMA) on these signaling proteins
demonstrate that the two signaling molecules from phosphatidylinositol
4,5-bisphosphate hydrolysis ([Ca2+]i, from
inositol 1,4,5-trisphosphate production, and diacylglycerol) can
individually initiate the activation of MAP kinase in an EGF
receptor-dependent manner. These results demonstrate that the
P2Y2 receptor-mediated transactivation of the EGF receptor occurs at a point downstream of RAFTK and indicate that the EGF receptor is required for P2Y2 receptor-mediated MAP
kinase activation. Although P2Y2 and EGF receptors may both
activate a similar multiprotein signaling cascade immediately upstream
of MAP kinase, the P2Y2 receptor appears to uniquely
utilize [Ca2+]i, PKC, and, subsequently,
RAFTK.
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