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J Biol Chem, Vol. 273, Issue 36, 22892-22898, September 4, 1998
q/11-induced Activation of c-Jun N-terminal Kinase and
p38 Mitogen-activated Protein Kinase
From the Faculty of Bioscience and Biotechnology, Tokyo Institute
of Technology, 4259 Nagatsuta-cho, Midori-ku,
Yokohama 226-8501, Japan
Mitogen-activated protein kinases (MAPKs) are
activated by various extracellular stimuli. The signaling pathways from
G protein-coupled receptors to extracellular signal-regulated kinase
have been partially elucidated, whereas the mechanisms by which G
protein-coupled receptors stimulate c-Jun N-terminal kinase (JNK) and
p38 MAPK activities remain largely unknown. We have recently
demonstrated that the signal from Gq/11-coupled m1
muscarinic acetylcholine receptor to p38 MAPK is mediated by both
G
q/11 and G
in HEK-293 cells (Yamauchi, J., Nagao,
M., Kaziro, Y., and Itoh, H. (1997) J. Biol. Chem.
272, 27771-27777). In the present study, we report that a
constitutively activated mutant of G11
(G11 Q209L) activated not only p38 MAPK, but also JNK,
and the activation of JNK and p38 MAPK by G11 Q209L was
partially inhibited by prolonged treatment with phorbol 12-myristate
13-acetate and calphostin C. In addition, the G11
Q209L-stimulated activation of both kinases was blocked by a specific
inhibitor of protein tyrosine kinases (PP2) and Csk
(C-terminal Src kinase).
Furthermore, we demonstrated that G11 Q209L stimulated
Src family kinase activity and induced tyrosine phosphorylation of
several proteins in HEK-293 cells. These results suggest that
Gq/11 stimulates JNK and p38 MAPK activities through protein kinase C- and Src family kinase-dependent signaling
pathways.
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