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Originally published In Press as doi:10.1074/jbc.M000312200 on March 24, 2000

J. Biol. Chem., Vol. 275, Issue 22, 16569-16573, June 2, 2000
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Stress-induced Activation of Protein Kinase CK2 by Direct Interaction with p38 Mitogen-activated Protein Kinase*

Mohamed SayedDagger , Sung O. KimDagger , Baljinder S. Salh§, Olaf-Georg Issinger, and Steven L. PelechDagger ||

From the Dagger  Department of Medicine, Koerner Pavilion, University of British Columbia, Vancouver, British Columbia V6T 1Z3, Canada, the § Department of Medicine, Jack Bell Research Centre, University of British Columbia, Vancouver, British Columbia V6H 3Z6, Canada, and the  Department of Biomedical Research and Molecular Cell Biology, Biokemisk Institut, SDU, Campusvej 55, 5230 Odense, Denmark

Protein kinase CK2 has been implicated in the regulation of a wide range of proteins that are important in cell proliferation and differentiation. Here we demonstrate that the stress signaling agents anisomycin, arsenite, and tumor necrosis factor-alpha stimulate the specific enzyme activity of CK2 in the human cervical carcinoma HeLa cells by up to 8-fold, and this could be blocked by the p38 MAP kinase inhibitor SB203580. We show that p38alpha MAP kinase, in a phosphorylation-dependent manner, can directly interact with the alpha  and beta  subunits of CK2 to activate the holoenzyme through what appears to be an allosteric mechanism. Furthermore, we demonstrate that anisomycin- and tumor necrosis factor-alpha -induced phosphorylation of p53 at Ser-392, which is important for the transcriptional activity of this growth suppressor protein, requires p38 MAP kinase and CK2 activities.

* This work was supported by a grant from the Medical Research Council of Canada and the National Cancer Institute of Canada (to S. L. P.).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: Dept. of Medicine, Room S125, 2nd Floor, Koerner Pavilion, 2211 Wesbrook Mall, University of British Columbia, Vancouver, B.C., V6T 1Z3, Canada. Tel.: 604-822-8086; Fax: 604-822-8693; E-mail: spelech@home.com.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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