Disease relevance of Csnk2a1

• The enhanced responses of ODC and of CK-II to DMH proceeded the actual polyp and tumor formation [1].

High impact information on Csnk2a1

• Molecular characterization revealed a 10-fold repeated motif of highly conserved acidic serine clusters that contain an abundance of phosphorylation consensus sites for casein kinase II (CK II) [2].
• Using this antibody, we showed that p53 is phosphorylated at the CK II site upon UV treatment of early passage rat embryo fibroblasts and RKO cells [3].
• These results indicate that phosphorylation at the CK II site is one of the post-translational mechanisms through which p53 is activated in response to UV radiation and that different mechanisms activate p53 after DNA damage by gamma radiation [3].
• CK-II activity was also selectively and rapidly augmented in another form of LTP produced by bath application of tetraethylammonium; this LTP (called LTPk) is Ca2+ dependent but N-methyl-D-aspartate independent [4].
• The stimulated protein kinase activity, which was blocked by a selective antagonist of N-methyl-D-aspartate receptors, exhibited specific properties of CK-II, including phosphorylation of the specific substrates of CK-II, marked inhibition by a low heparin concentration, and the use of GTP as a phosphate donor [4].

Biological context of Csnk2a1

• A glutamic acid cluster was located at the carboxyl-terminal side of Ser-11, showing the consensus sequence for phosphorylation by CK-II [5].
• RESULTS: AG34 inhibited the activity of CK II with IC50 33 (27-41) mumol.L-1 [6].

Anatomical context of Csnk2a1

• We now report that casein kinase II (CK-II), which is present in high concentration in the hippocampus, is also activated in the CA1 region during LTP [4].
• Based on the pattern of phosphorylation of the wildtype and two variant forms of eIF2B epsilon using casein kinase (CK)-I, CK-II, or GSK-3 as well as that observed with skeletal muscle extracts, we conclude that the predominant eIF2B epsilon kinase in psoas muscle is GSK-3 [7].

Associations of Csnk2a1 with chemical compounds

• Protein phosphatase-1 (PP-1) and -2A (PP-2A), two regulatory subunits of PP-1, the glycogen-binding subunit G and inhibitor-2 (I-2), kinase FA, and casein kinase II (CK-II) were investigated in skeletal muscle of diabetic rats 2 days after streptozotocin injection [8].
• The activity gradient of CK-II was markedly altered in DMH-treated cell populations: brisk activity of the kinase was observed in the upper crypt zone, the preserve of the mature, non-dividing colonocyte [1].
• Phosphorylation of casein or synthetic oligopeptides by CK-II was not affected by Ca2+, diolein, or phosphatidylserine [5].
• Since CK II is central in all these events, which are specifically affected by ethanol, the role of nuclear CK II is investigated in the present study [9].
• The polycations spermine and spermidine, bioactive molecules formed in the ODC-controlled polyamine pathway, were shown to markedly activate colonic CK-II [1].

Other interactions of Csnk2a1

• The activities of the growth-related enzymes ornithine decarboxylase (ODC) and casein kinase II (CK-II) were assayed along the colon crypt axis in a precise temporal sequence following administration of 1,2-dimethylhydrazine (DMH) to male rats [1].
• In activated cells, cPGES phosphorylation occurred in parallel with increased cPGES enzymic activity and PGE2 production from exogenous and endogenous arachidonic acid, and these processes were facilitated by Hsp90 (heat-shock protein 90), a molecular chaperone that formed a tertiary complex with cPGES and CK-II [10].

Analytical, diagnostic and therapeutic context of Csnk2a1

• CK-II activity increased within 2 min after a train of high-frequency electrical stimulations and reached a maximum (2-fold increase) 5 min later before returning to baseline value [4].

References