Disease relevance of CkIIbeta2

• The homologous NDPK's from Yeast and E. coli were also substrates for CK-2 in vitro, but not Drosophila NDPK [1].

High impact information on CkIIbeta2

• These results suggest a function for CK2-dependent phosphorylation in the molecular oscillator [2].
• Andante is a mutation of the gene encoding the beta subunit of CK2 and is predicted to perturb CK2beta subunit dimerization [2].
• The structure-activity relationship of casein kinase 2 (CK2) was examined with regard to its previously reported property to self-aggregate in vitro [3].
• Thus, CK2 may be considered as an associating-dissociating enzyme, and this remarkable property supports the hypothesis of a cooperative and allosteric regulation of the kinase in response to appropriate regulatory ligands possibly taking place in intact cells [3].
• We propose that the evolution and amplification of the novel chimeric gene have led to the overproduction of the regulatory CK2 subunit in testes [4].

Biological context of CkIIbeta2

• CK2 phosphorylation does not affect ATP hydrolysis by DmORC but modulates the ATP-dependent DNA-binding activity of DmORC [5].
• The Su(Ste) repeat in the Y chromosome and betaCK2tes gene encode predicted isoforms of regulatory beta-subunit of protein kinase CK2 in Drosophila melanogaster [6].
• CK2 and other clock genes have been implicated in cellular responses to DNA damage, particularly those induced by ultraviolet (UV) light [7].
• Our data show that native hetero tetrameric CK2 is a spermine binding protein and a spermine binding site was identified in the N-terminal region of the beta subunit of CK2 [8].
• In many respects, mutation of these phosphorylation sites phenocopies mutation of the catalytic subunit of CK2 [9].

Anatomical context of CkIIbeta2

• The X-linked Stellate repeats, encoding a putative regulatory subunit of protein kinase CK2, are expressed in XO male testes [10].

Associations of CkIIbeta2 with chemical compounds

• We report that this activity is inhibited in the presence of the serine/threonine protein kinase CK2 [11].
• Comparison of the effects of spermine and peptide beta 1-16 on CK2 structure and activity suggests that these two activating molecules may function in a different way [12].
• Substitution of the identified phosphoresidues by alanine was found to reduce considerably the ability of CK2 to phosphorylate NAP1 [13].
• Preincubation of CK2 with ATP/Mg2+ or GTP/Mg2+, but not adenosine/Mg2+ or Mg2+ alone, resulted in kinetics that were near linear [14].

Analytical, diagnostic and therapeutic context of CkIIbeta2

• Sequence analysis indicates that ZFP47 contains a consensus site for phosphorylation by CK2, 4 C1H1-type zinc-fingers, and a bipartite nuclear localization signal [15].

References