High impact information on CSNK2A2

• Addition of KN-62 or a synthetic peptide CK II, inhibitors of multifunctional Ca2+/calmodulin-dependent protein kinase II activity, abolished MLCK phosphorylation [1].
• Consistent with the properties of CK II, the peptide kinase activity was inhibited by very low concentrations of heparin (Ki less than 6 nM) and it used GTP efficiently as a substrate [2].
• The peptide Arg-Arg-Arg-Glu-Glu-Glu-Thr-Glu-Glu-Glu was shown to be a specific substrate for casein kinase II (CK II) in extracts of 3T3-L1 cells [2].
• A Western blot, developed with antiserum to bovine thymus CK II, demonstrated the presence of CK II protein in 3T3-L1 extracts and that peptide kinase activity was directly related to the amount of CK II protein [2].
• The peptide was used to assay CK II activity in extracts of 3T3-L1 cells stimulated to differentiate into adipocytes [2].

Biological context of CSNK2A2

• The casein kinase II alpha' gene (CSNK2A2), which physically maps to human chromosome 16 (HSA16), has previously been mapped to bovine chromosome 5 (BTA5) [3].
• Induction of CK II preceded the increase in total protein and was not the result of cell proliferation [2].
• We investigated the effect of synthetic A beta with the amino-acid sequence corresponding to cerebrovascular A beta and plaque A beta on the activities of casein kinase I (CK I) and casein kinase II (CK II) [4].

Anatomical context of CSNK2A2

• Casein kinase II (CK II) is a ubiquitous protein kinase that has been found in both nuclear and soluble subcellular fractions and whose precise cellular functions and mechanisms of control remain to be clarified [5].
• The experiments with synthetic CK II-substrate peptide (Leu-Glu-Leu-Ser-Asp-Asp-Asp-Asp-Glu) and the phosphorylation of erythrocyte membrane proteins by intrinsic membrane-bound CK I in erythrocytes showed marked stimulation in activities of casein kinases in the presence of A beta 1-40 or blocked A beta [4].
• Using a primer derived from T. parva CK II, we detected a parasite-specific CK II mRNA in T. parva-infected cell lines [6].

Associations of CSNK2A2 with chemical compounds

• Here we show that, in the usual CK-II assay, polylysine induces the aggregation of casein [7].
• The nuclear CK II uptake was dependent upon the presence of ATP and was stimulated by a kinase activator such as spermine, although the enzyme activity did not appear to be required for the process [5].
• Moreover the enzyme was found to be highly resistant to heparin, a potent inhibitor of casein kinase II (CK II) and also resistant to CK I-7, a synthetic inhibitor of CK I, but very sensitive to a bioflavonoid quercetin [8].
• Cells treated with 5,6-dichloro-1-beta-D-ribofuranosylbenzimidazole (DRB) are inhibited in a dose-dependent manner from under-going DNA synthesis as measured by [3H]-thymidine incorporation and from expressing CK II [6].
• The enzyme has been purified 370 fold and behaves catalytically as casein kinase type II, in the sense that it utilizes GTP as well as ATP as phosphoryl donors, it is inhibited by low heparin concentrations and phosphorylates a specific peptide for CK II [9].

References