Disease relevance of CSNK2B

• The greatest rates of phosphorylation were obtained with acidic phosphoprotein substrates such as casein or phosvitin, although potential physiological substrates for this activity included specific virion polypeptides of frog virus [1].
• Furthermore, when immature core subparticles which are enriched in Pr65gag are prepared from virions by Sepharose 6B exclusion column chromatography, about 50% of the kinase activity (as assayed with the exogenous substrate phosvitin) remains associated with the cores [2].
• We have found that in the presence of ATP and Mg2+, exogenously added substrates such as phosvitin and poly(Glu4-Tyr) are phosphorylated by intact K562 erythroleukemia, HL60 promyelocytic leukemia, and U937 histiocytic leukemia human cells [3].
• The enzyme, which uses both ATP and GTP as phosphoryl donors, catalyzes the phosphorylation of casein, phosvitin and E. coli RNA polymerase, but not of histone proteins [4].
• Establishment of human glioblastoma multiforme cell line, G5A [5].

High impact information on CSNK2B

• Fibrous apatite has been grown by the enzymatic hydrolysis of calcium beta-glycerophosphate on reconstituted calfskin collagen tapes which had been modified by the addition of a phosphoprotein, phosvitin, in the presence of a cross-linking agent, dimethylsuberimidate [6].
• The enzyme did not nucleotidylylate common casein kinase II substrates (casein, phosvitin) and the reaction was inhibited by heparin [7].
• The best available substrate for polypeptide-dependent protein kinase was beta-casein, and little or no phosphorylation was observed with alpha-casein, kappa-casein, phosvitin, alpha-lactalbumin, alpha-lactoglobulin, and histone [8].
• Cultured cells of different origin (rat liver, mouse cerebellum, and human lung) exhibited phosvitin-induced protein kinase release from intact cells [9].
• Chromatin-associated protein kinases active towards phosvitin, lysine-rich histone, and endogenous nonhistone proteins were characterized in human prostatic nuclei [10].

Biological context of CSNK2B

• Localization of eight additional genes in the human major histocompatibility complex, including the gene encoding the casein kinase II beta subunit (CSNK2B) [11].
• Both CSNK2A1 and CSNK2B mapped to known regions of conserved synteny between human and cattle, while CSNK2A2 defined a new homology segment between the human and bovine genomes [12].
• The alpha-subunit (CSNK2A1) was mapped to bovine chromosome 13, the alpha'-subunit (CSNK2A2) to chromosome 5 and the beta-subunit (CSNK2B) to chromosome 23 [12].
• At 1:1 molar ratio, CKII beta stimulated both catalytic subunits roughly fivefold with phosvitin as a substrate [13].
• In an attempt to purify and identify the kinase responsible for the phosphorylation of the 42 kDa protein, a casein-phosvitin affinity chromatography was used [14].

Anatomical context of CSNK2B

• Phosvitin, a highly phosphorylated glycoprotein, represents the major fraction of hen egg yolk phosphoproteins [15].
• It resembles phosvitin, a phosphoprotein present in the oocytes of nonmammalian vertebrates [16].
• Estrogen induced the appearance of phosvitin, lipovitellin, and apoVLDL-II in the blood plasma [17].
• Phosvitin introduced into nuclei of salivary gland cells becomes phosphorylated by the endogenous nuclear protein kinase(s) and incorporates phosphates from ATP as well as from GTP [18].
• There was a significant relationship of histone kinase but not phosvitin kinase activities with the number of spermatozoa originally present in the semen [19].

Associations of CSNK2B with chemical compounds

• Affinity chromatography of the concentrated ecto-PK through a heparin-matrix resolved two phosvitin/casein kinase activities upon elution with a NaCl gradient, termed as peak I and peak II [20].
• Affinity properties of phosvitin: interaction of phosvitin with serine hydroxymethyl transferase [21].
• The circular dichroism measurements suggest that phosvitin interaction does not involve pyridoxal phosphate binding domain of the enzyme [21].
• The protein kinase affected by DRB is cyclic AMP independent, prefers acidic protein substrates such as casein and phosvitin, and utilizes GTP as the phosphate donor almost as effectively as ATP in the phosphotransferase reaction [22].
• This protein, termed T-substrate, is far more effective than casein or phosvitin as a phosphoryl acceptor for a wheat germ kinase recently purified by our laboratory [23].

Physical interactions of CSNK2B

• Using electron spin resonance (ESR) with 5,5-dimethyl-1-pyrroline-N-oxide (DMPO) and deoxyribose degradation assays, we observed by both assays that phosvitin more effectively inhibited (.-)OH formation than iron-binding proteins such as ferritin and transferrin [24].

Enzymatic interactions of CSNK2B

• One abundant ecto-PK component is believed to be a protein kinase CKII since it phosphorylates phosvitin and casein, is sensitive to heparin at low concentrations, and can use both ATP and GTP as cosubstrate [20].
• Tightly adsorbed fractions possessed high troponin T kinase and phosvitin kinase activities and phosphorylated only serine-1 of troponin T. The results suggest that standard preparations of phosphorylase kinase are contaminated by troponin T kinase, which can phosphorylate serine-1 of troponin T [25].

Other interactions of CSNK2B

• Partial cDNA and complete exonic genomic sequencing of one of the new genes has identified it as the casein kinase II beta subunit (CSNK2B) [11].
• Thus, a three-component band fitting is used to characterize the Raman amide I band of alpha-synuclein, phosvitin, alpha-casein, beta-casein, and the non-A beta component (NAC) of Alzheimer's plaque [26].
• There are three phosphopeptides in the yolk: phosvitin (PV, 37.4 kDa) and phosvettes 1 (PVT1, 27.7 kDa) and 2 (PVT2, 26.1 kDa) [27].
• The amount of histatin 5 adsorbed was also found to increase as a function of the amount of phosvitin and statherin used to pre-coat HA up to a maximum level that was two- to four-fold greater than that observed on untreated HA [28].
• The A-431 membrane preparation also was capable of phosphorylating exogenous proteins, such as histone, phosvitin, and ribonuclease, by a process which was stimulated by EGF [29].

Analytical, diagnostic and therapeutic context of CSNK2B

• Human phosvitin/casein kinase type II. Molecular cloning and sequencing of full-length cDNA encoding subunit beta [30].
• The method is applied to microinjection studies with a monoclonal antibody against casein kinase II subunit beta [31].
• Determination of the dissociation constant of phosvitin-anti-phosphoserine interaction by affinity capillary electrophoresis [32].
• Histone kinase and phosvitin kinase activities were diminished 88% and 62%, respectively, in vasectomy seminal fluid [19].
• Native PAGE and gel filtration analyses showed that PV prevented an insolubilization of heat-denatured OT through ionic interactions [33].

References