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J. Biol. Chem., Vol. 275, Issue 36, 27634-27640, September 8, 2000
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From the The p38 mitogen-activated protein (MAP) kinase is
activated during engagement of the type I interferon (IFN) receptor and mediates signals essential for IFN
The Rac1/p38 Mitogen-activated Protein Kinase Pathway Is Required
for Interferon
-dependent Transcriptional Activation
but Not Serine Phosphorylation of Stat Proteins*
,,,,
,**
Section of Hematology-Oncology, University
of Illinois and West Side Veterans Administration Hospital, Chicago,
Illinois 60607, the § Division of Cell & Molecular Biology,
Toronto Research Institute, University Health Network and Department of
Immunology, University of Toronto, Toronto, Ontario M5S 3E2, Canada,
the ¶ Department of Cardiovascular Diseases, DuPont
Pharmaceuticals, Wilmington, Delaware 19880, and the Departments
of Immunology and Cell Biology, Scripps Research Institute, La Jolla,
California 92037
-dependent
transcriptional activation via interferon-stimulated response elements
without affecting formation of the ISGF3 complex. In the present study, we provide evidence that the small GTPase Rac1 is activated in a type I
IFN-dependent manner and that its function is required for
downstream engagement of the p38 MAP kinase pathway. We also demonstrate that p38 is required for IFN-dependent gene
transcription via GAS elements and regulates activation of the promoter
of the PML gene that mediates growth inhibitory responses. In
studies to determine whether the regulatory effects of p38 are mediated by serine phosphorylation of Stat1 or Stat3, we found that the p38
kinase inhibitors SB203580 or SB202190 or overexpression of a dominant
negative p38 mutant do not inhibit phosphorylation of Stat1 or Stat3 on
Ser-727 in several IFN-sensitive cell lines. Altogether these data
demonstrate that the Rac1/p38 MAP kinase signaling cascade plays a
critical role in type I IFN signaling, functioning in cooperation with
the Stat-pathway, to regulate transcriptional regulation of
IFN-sensitive genes and generation of growth inhibitory responses.
*
This work was supported by National Institutes of Health
Grants CA73381 and CA77816 (to L. C. P.), by a grant from the
Department of Veterans Affairs (to L. C. P.), and by Medical
Research Council of Canada Grant MT15094 (to E. N. F.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
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