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J. Biol. Chem., Vol. 269, Issue 40, 24666-24672, Oct, 1994
B VanRenterghem, MD Browning and JL Maller
Previously pp60v-src, cyclin A, p39mos, and maturation-promoting factor
(composed of Cdc2 and cyclin B) have been shown to activate mitogen-
activated protein kinase (MAPK) and MAPK kinase (MEK) in cell-free extracts
of Xenopus oocytes. The pp60v-src pathway is dependent on a functional Ras
signal whereas the cyclin/maturation-promoting factor pathway is not. Here
we show that protein kinase C (PKC) is also able to stimulate MAPK in a
Ras-dependent manner, but PKC is not necessary for signaling by pp60v-src.
In addition, preincubation of extracts with cAMP-dependent protein kinase
(PKA) blocks stimulation of MAPK by cyclin, p21V12ras, PKC, or pp60v-src,
by at least 50%, but stimulation by c-Mos is unaffected. Furthermore,
inhibition of endogenous PKA by the heat-stable PKA inhibitor is sufficient
to stimulate MAPK activity in these extracts in the absence of protein
synthesis and without dependence on a functional Ras protein. These results
suggest that independent pp60v-src and PKC pathways converge at Ras and
that PKA acts to block MAPK activation by both Ras-dependent and
-independent signals.
Regulation of mitogen-activated protein kinase activation by protein kinases A and C in a cell-free system
Department of Pharmacology, University of Colorado School of Medicine, Denver 80262.
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