Protein kinase CK2: an enzyme with multiple substrates and a puzzling regulation

Protein kinase CK2 (also known as casein kinase II) is a ubiquitous eukaryotic ser/thr protein kinase present in the nucleus and cytoplasm. CK2 is known to phosphorylate more than 100 substrates, many of which are involved in the control of cell division and in signal transduction. The review centers on the structure and function of CK2 α and β subunits and on the regulation of its activity, a topic that remains to be elucidated. An analogy is drawn between CK2 and the cyclin‐dependent kinases (cdks); both types of protein kinases share many substrates and are activated by regulatory subunits.—Allende, J. E., Allende, C. C. Protein kinase CK2: an enzyme with multiple substrates and a puzzling regulation. FASEB J. 9, 313–323 (1995)

[1]  M. Quadroni,et al.  Isolation of phosphorylated calmodulin from rat liver and identification of the in vivo phosphorylation sites. , 1994, The Journal of biological chemistry.

[2]  O. Issinger,et al.  Casein kinase 2 down-regulation and activation by polybasic peptides are mediated by acidic residues in the 55-64 region of the beta-subunit. A study with calmodulin as phosphorylatable substrate. , 1994, Biochemistry.

[3]  R. Pepperkok,et al.  Casein kinase II is required for transition of G0/G1, early G1, and G1/S phases of the cell cycle. , 1994, The Journal of biological chemistry.

[4]  O. Issinger,et al.  Efficient autophosphorylation and phosphorylation of the beta-subunit by casein kinase-2 require the integrity of an acidic cluster 50 residues downstream from the phosphoacceptor site. , 1994, The Journal of biological chemistry.

[5]  Activity of the E75E76 mutant of the α subunit of casein kinase II from Xenopus laevis , 1994 .

[6]  G. Draetta,et al.  The Schizosaccharomyces pombe casein kinase II alpha and beta subunits: evolutionary conservation and positive role of the beta subunit , 1994, Molecular and cellular biology.

[7]  H. Hameister,et al.  Expression of casein kinase 2 during mouse embryogenesis. , 1994, Acta anatomica.

[8]  O. Issinger,et al.  Reconstitution of normal and hyperactivated forms of casein kinase-2 by variably mutated beta-subunits. , 1993, Biochemistry.

[9]  A. Murray,et al.  The Cell Cycle: An Introduction , 1993 .

[10]  J. D. Etlinger,et al.  Copurification of casein kinase II with 20 S proteasomes and phosphorylation of a 30-kDa proteasome subunit. , 1993, The Journal of biological chemistry.

[11]  O. Bachs,et al.  Calmodulin can modulate protein phosphorylation in rat liver cells nuclei. , 1993, The Journal of biological chemistry.

[12]  S. Pongor,et al.  Activity of recombinant alpha and beta subunits of casein kinase II from Xenopus laevis. , 1993, Biochemistry.

[13]  O. Issinger,et al.  The autophosphorylation and p34cdc2 phosphorylation sites of casein kinase-2 beta-subunit are not essential for reconstituting the fully-active heterotetrameric holoenzyme. , 1993, Biochimica et biophysica acta.

[14]  P. Cohen,et al.  On target with a new mechanism for the regulation of protein phosphorylation. , 1993, Trends in biochemical sciences.

[15]  J. Ávila,et al.  Depletion of casein kinase II by antisense oligonucleotide prevents neuritogenesis in neuroblastoma cells. , 1993, The EMBO journal.

[16]  O. ole-MoiYoi,et al.  Evidence for the induction of casein kinase II in bovine lymphocytes transformed by the intracellular protozoan parasite Theileria parva. , 1993, The EMBO journal.

[17]  E. Nigg,et al.  Targets of cyclin-dependent protein kinases. , 1993, Current opinion in cell biology.

[18]  H. Voss,et al.  Human casein kinase II. The subunit alpha protein activates transcription of the subunit beta gene. , 1993, The Journal of biological chemistry.

[19]  Susan S. Taylor,et al.  A template for the protein kinase family. , 1993, Trends in biochemical sciences.

[20]  M. Hinrichs,et al.  Effect of metal ions on the activity of cascein kinase II from Xenopus laevis , 1993, FEBS letters.

[21]  O. Issinger,et al.  Casein kinases: pleiotropic mediators of cellular regulation. , 1993, Pharmacology & therapeutics.

[22]  R. Jakobi,et al.  Characterization of the phosphotransferase domain of casein kinase II by site-directed mutagenesis and expression in Escherichia coli. , 1992, The Journal of biological chemistry.

[23]  O. Issinger,et al.  Casein kinase-2 structure-function relationship: Creation of a set of mutants of the β subunit that variably surrogate the wildtype β subunit function , 1992 .

[24]  N. Osheroff,et al.  Effect of casein kinase II-mediated phosphorylation on the catalytic cycle of topoisomerase II. Regulation of enzyme activity by enhancement of ATP hydrolysis. , 1992, The Journal of biological chemistry.

[25]  B. Franza,et al.  Casein kinase II phosphorylates p34cdc2 kinase in G1 phase of the HeLa cell division cycle. , 1992, The Journal of biological chemistry.

[26]  C. Glover,et al.  Purification and characterization of casein kinase II (CKII) from delta cka1 delta cka2 Saccharomyces cerevisiae rescued by Drosophila CKII subunits. The free catalytic subunit of casein kinase II is not toxic in vivo. , 1992, The Journal of biological chemistry.

[27]  D. Brenner,et al.  Casein kinase II is a negative regulator of c-Jun DNA binding and AP-1 activity , 1992, Cell.

[28]  C. Allende,et al.  Folylpolyglutamate analogs can inhibit casein kinase II from Xenopus laevis , 1992, FEBS letters.

[29]  Tony Hunter,et al.  The regulation of transcription by phosphorylation , 1992, Cell.

[30]  T. Lindahl,et al.  Activation of mammalian DNA ligase I through phosphorylation by casein kinase II. , 1992, The EMBO journal.

[31]  E. Krebs,et al.  Phosphorylation of casein kinase II by p34cdc2 in vitro and at mitosis. , 1992, The Journal of biological chemistry.

[32]  S. Gasser,et al.  Casein kinase II phosphorylates the eukaryote‐specific C‐terminal domain of topoisomerase II in vivo. , 1992, The EMBO journal.

[33]  O. Issinger,et al.  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. , 1992, European journal of biochemistry.

[34]  M. Hinrichs,et al.  The cDNAs coding for the α‐ and β‐subunits of Xenopus laevis casein kinase II , 1992 .

[35]  O. Issinger,et al.  Role of the beta subunit of casein kinase-2 on the stability and specificity of the recombinant reconstituted holoenzyme. , 1992, European journal of biochemistry.

[36]  M. Cole,et al.  Casein kinase II inhibits the DNA-binding activity of Max homodimers but not Myc/Max heterodimers. , 1992, Genes & development.

[37]  R. Treisman,et al.  Casein kinase II phosphorylation increases the rate of serum response factor‐binding site exchange. , 1992, The EMBO journal.

[38]  E. Nigg,et al.  Casein kinase II is a predominantly nuclear enzyme , 1992, The Journal of cell biology.

[39]  P. Nurse,et al.  Animal cell cycles and their control. , 1992, Annual review of biochemistry.

[40]  O. Issinger,et al.  Cloning and sequencing of the casein kinase 2 α subunit from Zea mays , 1991 .

[41]  R. Pepperkok,et al.  Cell growth stimulation by EGF: inhibition through antisense-oligodeoxynucleotides demonstrates important role of casein kinase II. , 1991, Experimental cell research.

[42]  G. Dobrowolska,et al.  Benzimidazole nucleoside analogues as inhibitors of plant (maize seedling) casein kinases. , 1991, Biochimica et biophysica acta.

[43]  M. Czech,et al.  Enhanced casein kinase II activity in COS-1 cells upon overexpression of either its catalytic or noncatalytic subunit. , 1991, The Journal of biological chemistry.

[44]  P. Roach,et al.  Multisite and hierarchal protein phosphorylation. , 1991, The Journal of biological chemistry.

[45]  E. Palen,et al.  Phosphorylation of casein kinase II. , 1991, Biochemistry.

[46]  A. Varshavsky,et al.  The short-lived MAT alpha 2 transcriptional regulator is ubiquitinated in vivo. , 1991, Proceedings of the National Academy of Sciences of the United States of America.

[47]  R. Peters,et al.  The rate of nuclear cytoplasmic protein transport is determined by the casein kinase II site flanking the nuclear localization sequence of the SV40 T‐antigen. , 1991, The EMBO journal.

[48]  A. Murray,et al.  Cyclin is degraded by the ubiquitin pathway , 1991, Nature.

[49]  J. A. Traugh,et al.  Casein kinase I and II--multipotential serine protein kinases: structure, function, and regulation. , 1991, Advances in second messenger and phosphoprotein research.

[50]  S. Hanks,et al.  Protein kinase catalytic domain sequence database: identification of conserved features of primary structure and classification of family members. , 1991, Methods in enzymology.

[51]  C. Rubin,et al.  Expression of wild-type and mutated forms of the catalytic (alpha) subunit of Caenorhabditis elegans casein kinase II in Escherichia coli. , 1990, The Journal of biological chemistry.

[52]  J. Labbé,et al.  M-phase-specific cdc2 protein kinase phosphorylates the beta subunit of casein kinase II and increases casein kinase II activity. , 1990, European journal of biochemistry.

[53]  R. Moses,et al.  Expression of the cDNA for the beta subunit of human casein kinase II confers partial UV resistance on xeroderma pigmentosum cells. , 1990, Mutation research.

[54]  B. Vallee,et al.  Zinc coordination, function, and structure of zinc enzymes and other proteins. , 1990, Biochemistry.

[55]  M. Gatica,et al.  Copolymers of glutamic acid and tyrosine are potent inhibitors of oocyte casein kinase II , 1990, FEBS letters.

[56]  E. Krebs,et al.  Subunit structure of casein kinase II from bovine testis. Demonstration that the alpha and alpha' subunits are distinct polypeptides. , 1990, The Journal of biological chemistry.

[57]  E. Krebs,et al.  Myb DNA binding inhibited by phosphorylation at a site deleted during oncogenic activation , 1990, Nature.

[58]  N. Osheroff,et al.  Stimulation of casein kinase II by epidermal growth factor: relationship between the physiological activity of the kinase and the phosphorylation state of its beta subunit. , 1990, Proceedings of the National Academy of Sciences of the United States of America.

[59]  J. Maller,et al.  Biochemical characterization of the p34cdc2 protein kinase component of purified maturation-promoting factor from Xenopus eggs. , 1989, The Journal of biological chemistry.

[60]  Kathleen L. Gould,et al.  Tyrosine phosphorylation of the fission yeast cdc2+ protein kinase regulates entry into mitosis , 1989, Nature.

[61]  Susan S. Taylor,et al.  cAMP-dependent protein kinase. Model for an enzyme family. , 1989, The Journal of biological chemistry.

[62]  D. Marshak,et al.  Serum-stimulated cell growth causes oscillations in casein kinase II activity. , 1989, The Journal of biological chemistry.

[63]  K. Kandror,et al.  Casein kinase II from Rana temporaria oocytes. Intracellular localization and activity during progesterone-induced maturation. , 1989, European journal of biochemistry.

[64]  L. Pinna,et al.  Random tyrosine and glutamic acid-containing polymers are very powerful inhibitors of casein kinase-2. , 1989, Biochimica et biophysica acta.

[65]  M. Czech,et al.  Insulin-like growth factor I and insulin rapidly increase casein kinase II activity in BALB/c 3T3 fibroblasts. , 1988, The Journal of biological chemistry.

[66]  E. Krebs,et al.  Activation of multiple protein kinases during the burst in protein phosphorylation that precedes the first meiotic cell division in Xenopus oocytes. , 1988, The Journal of biological chemistry.

[67]  A. Wahba,et al.  Phosphorylation of the guanine nucleotide exchange factor from rabbit reticulocytes regulates its activity in polypeptide chain initiation. , 1988, Proceedings of the National Academy of Sciences of the United States of America.

[68]  R. Weinmann,et al.  The phosphorylation of nucleoplasmin by casein kinase‐2 is resistant to heparin inhibition , 1987, FEBS letters.

[69]  E. Krebs,et al.  Activation of casein kinase II in response to insulin and to epidermal growth factor. , 1987, Proceedings of the National Academy of Sciences of the United States of America.

[70]  M. Antonelli,et al.  Polylysine-containing peptides, including the carboxyl-terminal segment of the human c-Ki-ras 2 protein, affect the activity of some key membrane enzymes. , 1987, Proceedings of the National Academy of Sciences of the United States of America.

[71]  L. Pinna,et al.  Synthetic peptides including acidic clusters as substrates and inhibitors of rat liver casein kinase TS (type-2). , 1984, The Journal of biological chemistry.

[72]  A. Depaoli-Roach Synergistic phosphorylation and activation of ATP-Mg-dependent phosphoprotein phosphatase by F A/GSK-3 and casein kinase II (PC0.7). , 1984, The Journal of biological chemistry.

[73]  E. Chambaz,et al.  Oligomeric structure and catalytic activity of G type casein kinase. Isolation of the two subunits and renaturation experiments. , 1983, The Journal of biological chemistry.

[74]  J. Traugh,et al.  Kinetics of Phosphorylation of eIF-2 by the hemin-controlled repressor and casein kinase II. Inhibition by hemin and 2,3-diphosphoglyceric acid. , 1982, The Journal of biological chemistry.

[75]  G. Hathaway,et al.  Inhibition of casein kinase II by heparin. , 1980, The Journal of biological chemistry.

[76]  E. Chambaz,et al.  Adenosine 3',5'-monophosphate-independent protein kinase activities in the bovine adrenal cortex cytosol. , 1980, Endocrinology.

[77]  E. P. Kennedy,et al.  The enzymatic phosphorylation of proteins. , 1954, The Journal of biological chemistry.

[78]  I. Roussou The Schizosaccharomyces pombe Casein Kinase II a and ,B Subunits: Evolutionary Conservation and Positive Role of the Subunit , 2022 .

[79]  Arzobispo Morcillo Purification of a soluble casein kinase II from Dictyostelium discoideum lacking the fl subunit : regulation during proliferation and differentiation , 2022 .

[80]  Hartmut,et al.  Human Casein Kinase I 1 THE SUBUNIT a PROTEIN ACTIVATES TRANSCRIPTION OF THE SUBUNIT P GENE , 2022 .