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J Biol Chem, Vol. 274, Issue 6, 3772-3780, February 5, 1999
From ONYX Pharmaceuticals, Richmond, California 94806
Lysophosphatidic acid (LPA) stimulates the c-Fos
serum response element (SRE) by activating two distinct signal pathways
regulated by the small GTPases, Ras and RhoA. Ras activates the ERK
cascade leading to phosphorylation of the transcription factors Elk-1 and Sap1a at the Ets/TCF site. RhoA regulates an undefined pathway required for the activation of the SRF/CArG site. Here we have examined
the role of the Ras and RhoA pathways in activation of the SRE and
c-Fos expression in Rat-1 cells. Pertussis toxin and PD98059 strongly
inhibited LPA-stimulated c-Fos expression and activation of a SRE:Luc
reporter. C3 toxin completely inhibited RhoA function, partially
inhibited SRE:Luc activity, but had no effect on LPA-stimulated c-Fos
expression. Thus, in a physiological context the Ras-Raf-MEK-ERK
pathway, but not RhoA, is required for LPA-stimulated c-Fos expression
in Rat-1 cells. C3 toxin stimulated the stress-activated protein
kinases JNK and p38 and potentiated c-Jun expression and
phosphorylation; these properties were shared by another cellular
stress agonist the protein kinase C inhibitor Ro-31-8220. However, C3
toxin alone or in combination with growth factors did not stimulate
AP-1:Luc activity and actually antagonized the synergistic activation
of AP-1:Luc observed in response to co-stimulation with growth factors
and Ro-31-8220. These data indicate that C3 toxin is a cellular stress
which antagonizes activation of AP-1 at a point downstream of
stress-activated kinase activation or immediate-early gene induction.
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