Protein kinase CK2--a key suppressor of apoptosis.

Cellular and Molecular Biochemistry Research Laboratory (151), V.A. Medical Center, Department of Laboratory Medicine and Pathology, University of Minnesota, Minneapolis, MN 55417, USA.
Advances in enzyme regulation 05/2008; 48:179-87. DOI: 10.1016/j.advenzreg.2008.04.002
Source: PubMed
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    ABSTRACT: 2 folded plates in back pocket. Thesis (M.S.)--Idaho State University, 1987. Includes bibliographical references (leaves 90-96).
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    ABSTRACT: Casein kinase 2 (CK2), a highly conservative, multifunctional serine/threonine protein kinase, is critically important for the regulation of a plethora of processes in eukaryotes, such as cell proliferation, differentiation and death. CK2 is expressed in all tissues; in particular, its amount and activity are elevated in tumor cells. Unlike many regulatory proteins CK2 permanently adopts an active conformation. Of the utmost importance are the anti-apoptotic functions of CK2. This protein kinase is capable of regulating cell survival at multiple levels including DNA repair, NF-kappaB, Wnt, PI3K/Akt and JAK-STAT signaling cascades, chaperones, activation of anti-apoptotic proteins and down-regulation of pro-apoptotic counterparts, in particular, caspases. The versatility of CK2-mediated phosphorylation ensures the survival of tumor cells exposed to stimuli that differ in the origin and mechanisms of cytotoxicity. This manifold mode of CK2-dependent survival makes this enzyme an important target for antitumor therapy.
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