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J Biol Chem. 2000 Jun 2;275(22):16569-73.

Stress-induced activation of protein kinase CK2 by direct interaction with p38 mitogen-activated protein kinase.

Author information

1
Department of Medicine, Koerner Pavilion, University of British Columbia, Vancouver, British Columbia V6T 1Z3, Canada.

Abstract

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.

PMID:
10747897
DOI:
10.1074/jbc.M000312200
[Indexed for MEDLINE]
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