Stress-induced Activation of Protein Kinase CK2 by Direct Interaction with p38 Mitogen-activated Protein Kinase

• Published in: The Journal of biological chemistry 2000-06, Vol.275 (22), p.16569-16573
• Main Authors: Sayed, Mohamed, Kim, Sung O., Salh, Baljinder S., Issinger, Olaf-Georg, Pelech, Steven L.
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; anisomycin; Anisomycin - pharmacology; Arsenites - pharmacology; Casein Kinase II; CK2 protein; Enzyme Activation; Glutathione Transferase - metabolism; HeLa Cells; Humans; Imidazoles - pharmacology; mitogen-activated protein kinase; Mitogen-Activated Protein Kinases - antagonists & inhibitors; Mitogen-Activated Protein Kinases - metabolism; p38 Mitogen-Activated Protein Kinases; Protein-Serine-Threonine Kinases - metabolism; Pyridines - pharmacology; Recombinant Fusion Proteins - metabolism; Tumor Necrosis Factor-alpha - pharmacology
• ISSN: 0021-9258; 1083-351X
• DOI: 10.1074/jbc.M000312200

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-α 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 p38α MAP kinase, in a phosphorylation-dependent manner, can directly interact with the α and β subunits of CK2 to activate the holoenzyme through what appears to be an allosteric mechanism. Furthermore, we demonstrate that anisomycin- and tumor necrosis factor-α-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.