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Casein kinase II is a protein serine/threonine kinase that is thought to be present in all eukarotic cells, implying that it has fundamental cellular functions. The holoenzyme is a tetramer containing 2 alpha or alpha-prime subunits (or one of each) and 2 beta subunits. The function of beta subunits is unknown and the alpha subunit is the catalytic unit. CK2 functions as a tetrameric complex consisting of two regulatory beta-subunits and two catalytic units (alpha and alpha') in a homomeric or heteromeric conformation. Whilst the alpha- and alpha'-subunits are catalytically identical, proteins that regulate CK2, such as cdc2 and Hsp90, preferentially bind to the alpha and not the alpha'-subunit. CK2 can phosphorylate a number of key intracellular signaling proteins implicated in tumor suppression (p53 and PTEN) and tumorigenesis (myc, jun, NF-kappaB). CK2 is also thought to influence Wnt signaling via beta-catenin phosphorylation and the PI 3-K signaling pathway via the phosphorylation of Akt.
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