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J. Biol. Chem., Vol. 268, Issue 27, 19935-19938, 09, 1993
B VanRenterghem, JB Gibbs and JL Maller
In Xenopus oocytes, mitogen-activated protein (MAP) kinase can be activated
by progesterone treatment or by microinjection of cyclin A, both of which
lead to activation of the cdc2 protein kinase. The tyrosine kinase
pp60v-src has previously been shown to accelerate progesterone-induced
oocyte maturation and to increase the phosphorylation of ribosomal protein
S6 by pp90rsk, most likely by activating MAP kinase. In extracts of resting
oocytes, MAP kinase kinase and MAP kinase were activated by addition of
pp60v-src or cyclin A. Activation by pp60v-src was blocked by a
dominant-negative p21ras protein (RAST), but activation by cyclin A/cdc2
was unaffected. Thus these two pathways that converge at MAP kinase kinase
but are clearly divergent upstream of a p21ras-dependent step can be
studied in a cell- free system.
Reconstitution of p21ras-dependent and -independent mitogen-activated protein kinase activation in a cell-free system
Howard Hughes Medical Institute, University of Colorado School of Medicine, Denver 80262.
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