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J. Biol. Chem., Vol. 269, Issue 11, 7851-7854, Mar, 1994
M Faure, TA Voyno-Yasenetskaya and HR Bourne
Mitogen-activated protein kinases (MAPKs) are activated by a variety of
extracellular stimuli, including agonists for G protein-coupled receptors.
Using transient transfection of COS-7 cells, we have studied the
stimulation of a hemagglutinin-tagged p44mapk (p44HA-mapk) by receptors
coupled to Gs, Gq, and Gi. Agonists that act via all three G proteins
stimulated p44HA-mapk activity. A constitutively activated alpha s mutant,
forskolin, and a cAMP analog also increased p44HA-mapk activity, indicating
that cAMP in COS-7 cells, in contrast to other cell types, activates the
MAPK pathway. Similarly, a constitutively activated alpha q mutant,
overexpression of phospholipase C-beta 2, and a phorbol ester also
stimulated p44HA-mapk, suggesting that Gq-coupled receptors stimulate the
MAPK pathway by increasing phosphatidylinositol turnover and probably
stimulating protein kinase C. In COS-7 cells, in contrast to Rat-1 cells,
mutationally activated alpha i did not stimulate the MAPK pathway. G
protein beta and gamma subunits, overexpressed together, did activate
p44HA-mapk; this finding suggests that in COS-7 cells Gi-coupled receptors
may stimulate the MAPK pathway through beta gamma. These unexpected results
in COS-7 cells show that G proteins and second messengers regulate the MAPK
pathway differently in different cell types.
cAMP and beta gamma subunits of heterotrimeric G proteins stimulate the mitogen-activated protein kinase pathway in COS-7 cells
Department of Pharmacology, University of California, San Francisco 94143.
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