CK-2, a Multifunctional Protein Kinase and its Role during Proliferation
Casein kinase 2 (CK-2) is a second messenger-independent protein kinase consisting of two or three subunits which form a tetrameric complex, either αα′β2 or α2β2. The α subunits (mol. mass 44–46 kDa) represent the catalytic subunits of the enzyme, whereas the β subunit is non-catalytic with a molecular mass of 26 kDa. No specific modulator as for the cAMP-dependent protein kinase is known which can dissociate the subunits or regulate the enzyme. CK-2 is unique among the protein kinases in being able to use ATP as well as GTP as a phosphoryl donor. It phosphorylates preferentially serine or threonine residues surrounded by a cluster of acidic amino acid residues (XS/TXXEX).
KeywordsSucrose Urea Tyrosine Adenoma Serine
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- Boldyreff B, Schneider HR, Fritz G, Traffa K, Seitz G, Issinger OG (1989) CKII, a pleiotropic mediator of proliferation and oncogenesis. BioTechForum, Adv Mol Genet 2:91–98.Google Scholar
- Meggio F, Boldyreff B, Marin O, Marchiori F, Perich JW, Issinger OG, Pinna LA (1992) The effect of polylysine on casein kinase-2 activity is influenced by both the structure of the protein/peptide substrates and the subunit composition of the enzyme. Eur J Biochem 205:939–945.PubMedCrossRefGoogle Scholar
- Schneider HR, Issinger OG (1989) CKII, a multifunctional protein kinase and its role during proliferation, BiotechEurope 6, 1:82–88.Google Scholar