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J. Biol. Chem., Vol. 277, Issue 17, 14408-14416, April 26, 2002
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From the It is well established that engagement of the
Type I interferon (IFN) receptor results in activation of JAKs
(Janus kinases), which in turn regulate tyrosine phosphorylation
of STAT proteins. Subsequently, the IFN-dependent
tyrosine-phosphorylated/activated STATs translocate to the
nucleus to regulate gene transcription. In addition to tyrosine
phosphorylation, phosphorylation of Stat1 on serine 727 is essential
for induction of its transcriptional activity, but the
IFN
Protein Kinase C-
(PKC-) Is Activated by Type I Interferons
and Mediates Phosphorylation of Stat1 on Serine 727*
,,,,
Section of Hematology-Oncology, Department
of Medicine, University of Illinois at Chicago and West Side Veterans
Administration Medical Center, Chicago, Illinois 60607, the
¶ Department of Pharmacology, University of Illinois at Chicago,
Chicago, Illinois 60612, and the § Division of Cell and
Molecular Biology, Toronto General Research Institute, University
Health, Network and Department of Immunology, University of Toronto,
Toronto ON M5G2M1, Canada
-dependent serine kinase that regulates such
phosphorylation remains unknown. In the present study we provide
evidence that PKC-
, a member of the protein kinase C family of
proteins, is activated during engagement of the Type I IFN receptor and
associates with Stat1. Such an activation of PKC- appears to be
critical for phosphorylation of Stat1 on serine 727, as inhibition of
PKC- activation diminishes the IFN- or IFN
-dependent serine phosphorylation of Stat1. In
addition, treatment of cells with the PKC- inhibitor rottlerin or
the expression of a dominant-negative PKC- mutant results in
inhibition of IFN- and IFN-dependent gene
transcription via ISRE or GAS elements. Interestingly, PKC-
inhibition also blocks activation of the p38 MAP kinase, the function
of which is required for IFN-dependent transcriptional
regulation, suggesting a dual mechanism by which this kinase
participates in the generation of IFN responses. Altogether, these
findings indicate that PKC- functions as a serine kinase for Stat1
and an upstream regulator of the p38 MAP kinase and plays an important
role in the induction of Type I IFN-biological responses.
*
This work was supported by National Institutes of Health
Grants CA77816 and CA73381 (to L. C. P.), a Merit Review grant from the Department of Veterans Affairs (to L. C. P.), and Canadian Institutes of Health Research Grant MOP15094 (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.
To whom correspondence should be addressed: Section of
Hematology-Oncology, University of Illinois at Chicago, MBRB, MC-734, Rm. 3150, 900 S. Ashland Ave, Chicago, IL 60607. Tel.: 312-355-0155; Fax: 312-413-7963; E-mail: Lplatani@uic.edu.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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