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12 and G13 Regulate Extracellular Signal-regulated Kinase
and c-Jun Kinase Pathways by Different Mechanisms in COS-7 Cells
(Received for publication, April 18, 1996, and in revised form, June 6, 1996)
,
,
From the Many growth factors and agonists for G
protein-coupled receptors activate mitogen-activated protein (MAP)
kinase pathways, including the extracellular signal-regulated kinase
(ERK) pathway and the c-Jun kinase (JNK) pathway. Transient
transfection of dominant negative and constitutively active pathway
components in COS-7 cells shows that two G protein subunits, G
Department of Cellular and Molecular
Pharmacology and Medicine, Program in Cell Biology, and the
Cardiovascular Research Institute, University of California,
San Francisco, California 94143, and the ¶ Howard Hughes Medical
Institute, Department of Chemistry and Biochemistry, University of
Colorado, Boulder, Colorado 80309
12 and
G13, inhibit the ERK pathway and stimulate the JNK pathway.
Constitutively active (GTPase-deficient) G12 and G13
both inhibit ERK pathway activation by epidermal growth factor. A
G13/z chimera, which responds to stimulation by
Gi-coupled receptors, mediates inhibition of ERK via such a
receptor, the dopamine-2 receptor. In addition, expression of a
dominant negative mutant of the GTPase, Cdc42, blocks activation of the
JNK pathway by G12 and G13 but does not alter inhibition of ERK
activation by the same G proteins; conversely, mutationally
activated Cdc42 stimulates the JNK pathway but has no effect on the ERK
pathway. Our results show that different mechanisms mediate two effects
of G12 and G13: the ERK pathway inhibition is mediated at the
level of MAP kinase kinase in a Ras- and Raf-independent fashion,
whereas the JNK pathway stimulation is mediated by Cdc42.
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