Skip to main content
SpringerLink
Log in

Casein kinase II in signal transduction and cell cycle regulation

  • Protein Phosphorylation in Signal Transduction
  • Published:
Molecular and Cellular Biochemistry Aims and scope Submit manuscript

Abstract

Casein kinase II is a protein serine/threonine kinase that is ubiquitously distributed in eukaryotes. Molecular cloning studies and protein sequence analysis of purified proteins have demonstrated the existence of two related, but distinct, isozymic forms of its catalytic subunit in mammals and birds. At present, the precise role of the individual casein kinase II isoforms in biological responses is poorly understood. However, a great deal of evidence indicates that casein kinase II is an important component of signalling pathways that control the growth and division of cells. In particular, casein kinase II is known to phosphorylate, and in several cases, regulate the activity of a variety of regulatory nuclear proteins including nuclear oncoproteins, transcription factors, and enzymes involved in other aspects of DNA metabolism. In this review, we will summarize evidence relating to the involvement of casein kinase II in signal transduction events that are relevant to cell proliferation.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Log in via an institution

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Similar content being viewed by others

References

  1. Edelman AM, Blumenthal DK, Krebs EG: Protein serine/threonine kinases. Ann Rev Biochem 56: 657–613, 1987

    Google Scholar 

  2. Hunter T: A thousand and one protein kinases. Cell 50: 823–829, 1987

    PubMed  Google Scholar 

  3. Cohen P: The structure and regulation of protein phosphatases. Ann Rev Biochem 58: 453–508, 1989

    PubMed  Google Scholar 

  4. Pelech SL, Sanghera JS, Daya-Makin M: Protein kinase cascades in meiotic and mitotic cell cycle control. Biochem Cell Biol 68: 1297–1330, 1990

    PubMed  Google Scholar 

  5. Norbury C, Nurse P: Animal cell cycles and their control. Ann Rev Biochem 61: 441–470, 1992

    PubMed  Google Scholar 

  6. Ahn NG, Seger R, Krebs EG: The mitogen-activated protein kinase activator. Curr op Cell Biol 4: 992–999, 1992

    PubMed  Google Scholar 

  7. Hunter T, Karin M: The regulation of transcription by phosphorylation. Cell 70: 375–387, 1992

    PubMed  Google Scholar 

  8. Tuazon PT, Traugh JA: Casein kinase I and II-Multipotential serine protein kinases structure, function and regulation. Adv Sec Mess Phos Res 23: 123–164, 1991

    Google Scholar 

  9. Pinna LA: Casein kinase 2: an ‘eminence grise’ in cellular regulation? Biochim Biophys Acta 1054: 267–284, 1990

    PubMed  Google Scholar 

  10. Meisner H, Czech MP: Phosphorylation of transcriptional factors and cell-cycle-dependent proteins by casein kinase II. Curr Op Cell Biol 3: 474–483, 1991

    PubMed  Google Scholar 

  11. Krebs EG, Eisenman RN, Kuenzel EA, Litchfield DW, Lozeman FJ, Lüscher B, Sommercorn J: Casein kinase II as a potentially important enzyme concerned with signal transduction. Cold Spring Harbor Symp Quant Biol 53: 77–84, 1988

    PubMed  Google Scholar 

  12. Chen-Wu JL-P, Padmanabha R, Glover CVC: Isolation, sequencing and disruption of the CKA1 gene encoding the alpha subunit of yeast casein kinase II. Mol Cell Biol 8: 4981–4990, 1988

    PubMed  Google Scholar 

  13. Padmanabha R, Chen-Wu JL-P, Hanna DE, Glover CVC: Isolation, sequencing and disruption of the yeast CKA2 gene: casein kinase II is essential for viability in Saccharomyces cerevisiae. Mol Cell Biol 10: 4089–4099, 1990

    PubMed  Google Scholar 

  14. Meisner H, Heller-Harrison R, Buxton J, Czech MP: Molecular cloning of the human casein kinase II α subunit. Biochemistry 28: 4072–4076, 1989

    PubMed  Google Scholar 

  15. Lozeman FJ, Litchfield DW, Piening C, Takio K, Walsh KA, Krebs EG: Isolation and characterization of human cDNA clones encoding the α and α' subunits of casein kinase II. Biochemistry 29: 8436–8447, 1990

    PubMed  Google Scholar 

  16. Maridor G, Park W, Krek W, Nigg EA: Casein kinase II: cDNA sequences, developmental expression, and tissue distribution of mRNAs for α, α' and β subunits of the chicken enzyme. J Biol Chem 266: 2362–2368, 1987

    Google Scholar 

  17. Takio K, Kuenzel EA, Walsh KA, Krebs EG: Amino acid sequence of the β subunit of bovine lung casein kinase II. Proc Natl Acad Sci USA 84: 4851–4855, 1987

    PubMed  Google Scholar 

  18. Litchfield DW, Lozeman FJ, Piening C, Sommercorn J, Takio K, Walsh KA, Krebs EG: Subunit structure of casein kinase II from bovine testis: demonstration that the α and α' subunits are distinct polypeptides. J Biol Chem 265:7638–7644, 1990

    PubMed  Google Scholar 

  19. Hanks SK, Quinn AM: Protein kinase catalytic domain sequence database: identification of conserved features of primary structure and classification of family members. Methods Enzymol 200: 38–62, 1991

    PubMed  Google Scholar 

  20. Saxena A, Padmanabha R, Glover CVC: Isolátion and sequencing of cDNA clones encoding alpha and beta subunits of Drosophila melanogaster casein kinase II. Mol Cell Biol 7:3409–3417, 1987

    PubMed  Google Scholar 

  21. Jakobi R, Voss H, Pyerin W: Human phosvitin/casein kinase type II: molecular cloning and sequencing of full-length cDNA encoding subunit beta. Eur J Biochem 183:227–233, 1989

    PubMed  Google Scholar 

  22. Heller-Harrison RA, Meisner H, Czech MP: Cloning and characterization of a cDNA encoding the β subunit of human casein kinase II. Biochemistry 28:9053–9058, 1989

    PubMed  Google Scholar 

  23. Hu E, Rubin CS: Casein kinase II from Caenorhabditis elegans: cloning, characterization, and developmental regulation of the gene encoding the β subunit. J Biol Chem 266:19796–19802, 1991

    PubMed  Google Scholar 

  24. Boldyreff B, Piontek K, Schmidt-Spaniol I, Issinger O-G: The β subunit of casein kinase II: cloning of cDNAs from murine and porcine origin and expression of the porcine sequence as a fusion protein. Biochim Biophys Acta 1088: 439–441, 1991

    PubMed  Google Scholar 

  25. Teitz T, Eli D, Penner M, Bakhanashivili M, Naiman T, Timme TL, Wood CM, Moses RE, Canaani D: Expression of the cDNA for the beta subunit of casein kinase II confers partial UV resistance on xeroderma pigmentosum cells. Mutation Res 236:85–97, 1990

    PubMed  Google Scholar 

  26. Kopatz I, Naiman T, Eli D, Cananni D: The nucleotide sequence of the mouse cDNA encoding the beta subunit of CKII. Nuc Acid Res 18:3639, 1990

    Google Scholar 

  27. Jedlicki A, Hinrichs MV, Allende CC, Allende JE: The cDNAs coding for the α and β subunits of Xenopus laevis casein kinase II. FEBS Lett 297:280–284, 1992

    PubMed  Google Scholar 

  28. Livak KJ: Detailed structure of the Drosophila melanogaster stellate genes and their transcripts. Genetics 124:303–316, 1990

    PubMed  Google Scholar 

  29. Cochet C, Chamboaz EM: Oligomeric structure and catalytic activity of G type casein kinase. J Biol Chem 258: 1403–1406, 1983

    PubMed  Google Scholar 

  30. Hu E, Rubin CS: Expression of wild-type and mutated forms of the catalytic (α) subunit of Caenorhabditis elegans casein kinase II in Escherichia coli. J Biol Chem 265: 20609–20615, 1990

    PubMed  Google Scholar 

  31. Lin W-J, Tuazon PT, Traugh JA: Characterization of the catalytic subunit of casein kinase II expressed in Escherichia coli and regulation of activity J Biol Chem 266: 5664–5669, 1991

    PubMed  Google Scholar 

  32. Meggio F, Boldyreff B, Marin O, Pinna LA, Issinger O-G: Role of the β subunit of casein kinase-2 on the stability and specificity of the recombinant reconstituted holoenzyme. Eur J Biochem 204: 293–297, 1992

    PubMed  Google Scholar 

  33. Grankowski N, Boldryreff B, Issinger O-G: Isolation and characterization of recombinant human casein kinase II subunits α and β from bacteria. Eur J Biochem 198: 25–30, 1991

    PubMed  Google Scholar 

  34. Filhol O, Cochet C, Wedegaertner P, Gill GN, Chambaz EM: Coexpression of both α and β subunits is required for assembly of regulated casein kinase II. Biochemistry 30: 11133–11140, 1991

    PubMed  Google Scholar 

  35. Heller-Harrison RA, Czech MP: Enhanced casein kinase II activity in COS-1 cells upon overexpression of either its catalytic or noncatalytic subunit. J Biol Chem 266: 14435–14439, 1991

    PubMed  Google Scholar 

  36. Boldyreff B, Meggio F, Pinna LA, Issinger O-G: Casein kinase 2 structure function relationship: creation of a set of mutants of the β subunit that variably surrogate the wildtype β subunit function. Biochem Biophys Res Commun 188: 228–234, 1992

    PubMed  Google Scholar 

  37. Litchfield DW, Lozeman FJ, Cicirelli MF, Harrylock M, Ericsson LH, Piening CJ, Krebs EG: Phosphorylation of the β subunit of casein kinase II in human A431 cells: identification of the autophosphorylation site and a site phosphorylated by p34cdc2. J Biol Chem 266: 20380–20389, 1991

    PubMed  Google Scholar 

  38. Lüscher B, Litchfield DW: Biosynthesis of casein kinase II. Submitted for publication

  39. Meggio F, Perich JW, Johns RB, Pinna LA: Partially dephosphorylated phosphopeptide AcSer(P)-Ser(P)-Ser(P) is an excellent substrate for casein kinase-2. FEBS Lett 237: 225–228, 1988

    PubMed  Google Scholar 

  40. Hrubey TW, Roach PJ: Phosphoserine in peptide substrates can specify casein kinase II action. Biochem Biophys Res Commun 172: 190–196, 1990

    PubMed  Google Scholar 

  41. Litchfield DW, Arendt A, Lozeman FJ, Krebs EG, Hargrave PA, Palczewski KP: Synthetic phosphopeptides are substrates for casein kinase II. FEBS Lett 261: 117–120, 1990

    PubMed  Google Scholar 

  42. Meggio F, Perich JW, Reynolds EC, Pinna LA: Phosphotyrosine as a specificity determinant for casein kinase-2, a growth related Ser/Thr-specific protein kinase. FEBS Lett 279: 307–309, 1991

    PubMed  Google Scholar 

  43. Marin O, Meggio F, Draetta G, Pinna LA: The consensus sequences for cdc2 kinase and for casein kinase-2 are mutually incompatible. FEBS Lett 301: 111–114, 1992

    PubMed  Google Scholar 

  44. Perich JW, Meggio F, Reynolds ER, Marin O, Pinna LA: Role of phosphorylated aminoacyl residues in generating atypical consensus sequences which are recognized by casein kinase-2 but not by casein kinase 1. Biochemistry 31: 5893–5897, 1992

    PubMed  Google Scholar 

  45. Roach PJ: Multisite and hierarchal protein phosphorylation. J Biol Chem 266: 14139–14142, 1991

    PubMed  Google Scholar 

  46. Pfaff M, Anderer FA: Casein kinase II accumulation in the nucleolus and its role in nucleolar phosphorylation. Biochim Biophys Acta 969: 100–109, 1988

    PubMed  Google Scholar 

  47. Belenguer P, Baldin V, Mathieu C, Prats H, Bensaid M, Bouche G, Amalric F: Protein kinase NII and the regulation of rDNA transcription in mammalian cells. Nuc Acids Res 17: 6625–6636, 1989

    Google Scholar 

  48. Filhol O, Cochet C, Chambaz EM: Cytoplasmic and nuclear distribution of casein kinase II: characterization of the enzyme uptake by bovine adrenocortical nuclear preparation. Biochemistry 29: 9928–9936, 1990

    PubMed  Google Scholar 

  49. Lorenz P, Pepperkok R, Ansorge W, Pyerin W: Cell biological studies with monoclonal and polyclonal antibodies against human casein kinase II subunit β demonstrate participation of the kinase in mitogenic signaling. J Biol Chem 268: 2733–2739, 1993

    PubMed  Google Scholar 

  50. Yu IJ, Spector DL, Base Y-S, Marshak DR: Immunocytochemical localization of casein kinase II during interphase and mitosis. J Cell Biol 114: 1217–1232, 1991

    PubMed  Google Scholar 

  51. Krek W, Maridor G, Nigg EA: Casein kinase II is a predominantly nuclear enzyme. J Cell Biol 116: 43–55, 1992

    PubMed  Google Scholar 

  52. Prowald K, Fischer H, Issinger O-G: Enhanced casein kinase II activity in human tumour cell cultures. FEBS Lett 176: 479–483, 1984

    PubMed  Google Scholar 

  53. Münstermann U, Fritz G, Seitz G, Yiping L, Schneider HR, Issinger O-G: Casein kinase II is elevated in solid human tumours and rapidly proliferating non-neoplastic tissue. Eur J Biochem 189: 251–257, 1990

    PubMed  Google Scholar 

  54. Birnbaum MJ, Glover CVC: The phosphotransferase activity of casein kinase II is required for its physiological functionin vivo. Biochem Biophys Res Commun 181: 524–528, 1991

    PubMed  Google Scholar 

  55. Kikkawa U, Mann SKO, Firtel RA, Hunter T: Molecular cloning of casein kinase α subunit from Dictyostelium discoideum and its expression in the life cycle. Mol Cell Biol 12: 5711–5723, 1992

    PubMed  Google Scholar 

  56. Pepperkok R, Lorenz P, Jakobi R, Ansorge W, Pyerin W: Cell growth stimulation by EGF: inhibition through antisense-oligodeoxynucleotides demonstrates important role of casein kinase II. Exp Cell Res 197: 245–253, 1991

    PubMed  Google Scholar 

  57. Pyerin W, Pepperkok R, Ansorge W, Lorenz P: Early cell growth stimulation is inhibited by casein kinase II antisense oligodeoxynucleotides. Ann NY Acad Sci 650: 295–298, 1992

    Google Scholar 

  58. Gauthier-Rouviere C, Basset M, Blanchard J-M, Cavadore J-C, Fernandez A, Lamb NJC: Casein kinase II induces c-fos expression via the serum response element pathway and p67SRF phosphorylation in living fibroblasts. EMBO J 10: 2921–2930, 1991

    PubMed  Google Scholar 

  59. Lin A, Frost J, Deng T, Smeal T, Al-Alawi N, Kikkawa U, Hunter T, Brenner D, Karin M: Casein kinase II is a negative regulator of c-Jun DNA binding and AP-1 activity. Cell 70: 777–789, 1992

    PubMed  Google Scholar 

  60. Lüscher B, Kuenzel EA, Krebs EG, Eisenman RN: Myc oncoproteins are phosphorylated by casein kinase II. EMBO J 8: 1111–1119, 1989

    PubMed  Google Scholar 

  61. Street AJ, Blackwood E, Lüscher B, Eisenman RN: Mutational analysis of the carboxy-terminal casein kinase II phosphorylation site in human c-Myc. Curr Top Micro Immunol 166: 251–258, 1990

    Google Scholar 

  62. Hamann U, Wenzel A, Frank R, Schwab M: The MYCN protein of human neuroblastoma cells is phosphorylated by casein kinase II in the central region and at serine 367. Oncogene 6: 1745–1751, 1991

    PubMed  Google Scholar 

  63. Hagiwara T, Nakaya K, Nakamura Y, Nakajima H, Nishimura S, Taya Y: Specific phosphorylation of the acidic central region of the N-Myc protein by casein kinase II. Eur J Biochem 209: 945–950, 1992

    PubMed  Google Scholar 

  64. Glineur C, Bailly M, Ghysdael J: The c-erb A α-encoded thyroid hormone receptor is phosphorylated in its amino terminal domain by casein kinase II. Oncogene 4: 1247–1254, 1989

    PubMed  Google Scholar 

  65. Blackwood EM, Eisenman RN: Max: a helix-loop-helix zipper protein that forms a sequence-specific DNA-binding complex with myc. Science 251: 1211–1217, 1991

    PubMed  Google Scholar 

  66. Blackwood EM, Lüscher B, Eisenman RN: Myc and Max associatein vivo. Genes & Dev 6: 71–80, 1992

    Google Scholar 

  67. Berberich SJ, Cole MD: Casein kinase II inhibits the DNA-binding of Max homodimers but not Myc/Max heterodimers. Genes & Dev 6: 166–176, 1992

    Google Scholar 

  68. Bousset K, Henriksson M, Lüscher-Firzlaff JM, Litchfield DW, Lüscher B: Identification of casein kinase II phosphorylation sites in Max: Effects on DNA-binding kinetics of Max homo- and Myc/Max heterodimers. Oncogene, in press

  69. Lüscher B, Christenson E, Litchfield DW, Krebs EG, Eisenman RN: Myb DNA binding inhibited by phosphorylation at a site deleted during oncogenic activation. Nature 344: 517–522, 1990

    PubMed  Google Scholar 

  70. Manak JR, Bisschop N, Kris RM, Prywes R: Casein kinase II enhances the DNA binding activity of serum response factor. Genes & Dev 4: 955–967, 1990

    Google Scholar 

  71. Marais RM, Hsuan JJ, McGuigan C, Wynne J, Treisman R: Casein kinase II phosphorylation increases the rate of serum response factor-binding site exchange. EMBO J 11: 97–105, 1992

    PubMed  Google Scholar 

  72. Janknecht R, Hipskind RA, Houthaeve T, Nordheim A, Stunnenberg HG: Identification of multiple SRF N-terminal phosphorylation sites affecting DNA binding properties. EMBO J 11: 1045–1054, 1992

    PubMed  Google Scholar 

  73. Manak JR, Prywes R: Phosphorylation of serum response factor by casein kinase II: evidence against a role in growth factor regulation of fos expression. Oncogene 8: 703–711, 1993

    PubMed  Google Scholar 

  74. Milne DM, Palmer RH, Meek DW: Mutation of the casein kinase II phosphorylation site abolishes the anti-proliferative activity of p53. Nuc Acid Res 20: 5565–5570, 1992

    Google Scholar 

  75. Hupp TR, Meek DW, Midgely CA, Lane DP: Regulation of the specific DNA binding function of p53. Cell 71: 875–886, 1992

    PubMed  Google Scholar 

  76. Meek DW, Simon S, Kikkawa U, Eckhart WL: The p53 tumour suppressor protein is phosphorylated at serine 389 by casein kinase II. EMBO J 9: 3253–3260, 1990

    PubMed  Google Scholar 

  77. Herrmann CPE, Kraiss S, Montenarh M: Association of casein kinase II with immunopurified p53. Oncogene 6: 877–884, 1991

    PubMed  Google Scholar 

  78. Filhol O, Baudier J, Delphin C, Loue-Mackenbach P, Chambaz EM, Cochet C: Casein kinase II and the tumour suppressor protein p53 associate in a molecular complex that is negatively regulated upon p53 phosphorylation. J Biol Chem 267: 20577–20583, 1992

    PubMed  Google Scholar 

  79. Vogelstein B, Kinzler KW: p53 function and dysfunction. Cell 70: 523–526, 1992

    PubMed  Google Scholar 

  80. Pongubala JMR, Van Beveren C, Nagulapalli S, Klemsz MJ, McKercher SR, Maki RA, Atchison ML: Effect of PU.1 phosphorylation on interaction with NF-EM5 and transcriptional activation. Science 259: 1622–1625, 1993

    PubMed  Google Scholar 

  81. Voit R, Schnapp A, Kuhn A, Rosenbauer H, Hirschmann P, Stunnenberg HG, Grummt I: The nucleolar transcription factor mUBF is phosphorylated by casein kinase II in the C-terminal hyperacidic tail which is essential for transactivation. EMBO J 11: 2211–2218, 1992

    PubMed  Google Scholar 

  82. O'Mahony DJ, Smith SD, Xie WQ, Rothblum LI: Analysis of the phosphorylation, DNA-binding and dimerization properties of the RNA polymerase 1 transcription factors UBF1 and UBF2. Nuc Acid Res 20: 1301–1308, 1992

    Google Scholar 

  83. Prigent C, Lasko DD, Kodama K, Woodgett JR, Lindahl T: Activation of mammalian DNA ligase 1 through phosphorylation by casein kinase II. EMBO J 11: 2925–2933, 1992

    PubMed  Google Scholar 

  84. Corbett AH, DeVore RF, Osheroff N: Effect of casein kinase II-mediated phosphorylation on the catalytic cycle of Topoisomerase II. J Biol Chem 267: 20513–20518, 1992

    PubMed  Google Scholar 

  85. Cardenas ME, Dang Q, Glover CVC, Gasser SM: Casein kinase II phosphorylates the eukaryote-specific C-terminal domain of topoisomerase IIin vivo. EMBO J 11: 1785–1796, 1992

    PubMed  Google Scholar 

  86. Grasser FA, Scheidtmann KH, Tuazon PT, Traugh JA, Walter G:In vitro phosphorylation of SV40 large T antigen. Virology 165: 13–22, 1988

    PubMed  Google Scholar 

  87. Rihs H-P, Jans DA, Fan H, Peters R: The rate of cytoplasmic protein transport is determined by the casein kinase II site flanking the nuclear localization sequence of the SV40 T-antigen. EMBO J 10: 633–639, 1991

    PubMed  Google Scholar 

  88. Firzlaff JM, Galloway DA, Eisenman RN, Lüscher B: The E7 protein of human papillomavirus type 16 is phosphorylated by casein kinase II. New Biol 1: 44–53, 1989

    PubMed  Google Scholar 

  89. Barbosa MS, Edmonds C, Fisher C, Schiller JT, Lowy DR, Voudsen KH: The region of the HPV E7 oncoprotein homologous to adenovirus E1a and SV40 large T antigen contains separate domains for Rb binding and casein kinase II phosphorylation. EMBO J 9: 153–160, 1990

    PubMed  Google Scholar 

  90. Firzlaff JM, Lüscher B, Eisenman RN: Negative charge at the casein kinase II phosphorylation site is important for transformation but not for Rb protein binding by the E7 protein of human papillomavirus type 16. Proc Natl Acad Sci USA 88: 5187–5191, 1991

    PubMed  Google Scholar 

  91. Carroll D, Marshak DR: Serum-stimulated cell growth causes oscillations in casein kinase II activity. J Biol Chem 264: 7345–7348, 1989

    PubMed  Google Scholar 

  92. Cicirelli MF, Pelech SL, Krebs EG: Activation of multiple protein kinases during the burst in protein phosphorylation that precedes the first meiotic cell division in Xenopus oocytes. J Biol Chem 263: 2009–2019, 1988

    PubMed  Google Scholar 

  93. Mulner-Lorillon O, Marot JM, Cayla X, Poùhle R, Belle R: Purification and characterization of a casein kinase-II-type enzyme from Xenopus laevis ovary. Eur J Biochem 171: 107–117, 1988

    PubMed  Google Scholar 

  94. Kandror KV, Benumov AO, Stepanov AS: Casein kinase II from Rana temporaria oocytes: intracellular localization and activity during progesterone-induced maturation. Eur J Biochem 180: 441–448, 1989

    PubMed  Google Scholar 

  95. Pelech SL, Sanghera JS, Paddon HB, Quayle KA, Brownsey RW: Identification of a major maturation-activated acetyl-CoA carboyxlase kinase in sea star oocytes as p44mpk. Biochem J 274: 759–767, 1991

    PubMed  Google Scholar 

  96. Sommercorn J, Mulligan JA, Lozeman FJ, Krebs EG: Activation of casein kinase II in response to insulin and to epidermal growth factor. Proc Natl Acad Sci USA 84: 8834–8838, 1987

    PubMed  Google Scholar 

  97. Klarlund JK, Czech MP: Insulin-like growth factor I and insulin rapidly increase casein kinase II activity in Balb/c 3T3 fibroblasts. J Biol Chem 263: 15872–15875, 1988

    PubMed  Google Scholar 

  98. Maeda R, Raz I, Zurlo F, Sommercorn J: Activation of skeletal muscle casein kinase II by insulin is not diminished in subjects with insulin resistance. J Clin Invest 87: 1017–1022, 1991

    PubMed  Google Scholar 

  99. Villa-Moruzzi E, Crab JW: Stimulation of FA and casein kinase II by insulin in 3T3-L1 cells. Biochem Biophys Res Commun 177: 1019–1024, 1991

    PubMed  Google Scholar 

  100. Diggle TA, Schmitz-Peiffer C, Borthwick AC, Welsh GI, Denton RM: Evidence that insulin activates casein kinase II in rat epididymal fat-cells and that this may result in the increased phosphorylation of an acid-soluble 22 kDa protein. Biochem J 279: 545–551, 1991

    PubMed  Google Scholar 

  101. Ackerman P, Osheroff N: Regulation of casein kinase II activity by epidermal growth factor in human A431 carcinoma cells. J Biol Chem 264: 11958–11965, 1989

    PubMed  Google Scholar 

  102. Ackerman P, Glover CVC, Osheroff N: Stimulation of casein kinase II by epidermal growth factor: relationship between the physiological activity of the kinase and the phosphorylation state of its β subunit. Proc Natl Acad Sci USA 87: 821–825, 1990

    PubMed  Google Scholar 

  103. Agostinis P, Van Lint J, Sarno S, DeWitte P, Vandenheede JR, Merlevede W: Rapid stimulation of Ser/Thr protein kinase following treatment of Swiss 3T3 cells with bombesin: involvement of casein kinase II in the signaling pathway of bombesin. J Biol Chem 267: 9732–9737, 1992

    PubMed  Google Scholar 

  104. Van Lint J, Agostinis P, Vandevoorde V, Haegeman G, Fiers W, Merlevede W, Vandenheede JR: Tumour necrosis factor stimulates multiple serine/threonine protein kinases in Swiss 3T3 and L929 cells: implication of casein kinase II and extracellular signal-regulated kinases in the tumour necrosis factor signal transduction pathway. J Biol Chem 267: 25916, 25921, 1992

    PubMed  Google Scholar 

  105. Haystead TAJ, Weiel JE, Litchfield DW, Tsukitani Y, Fischer EH, Krebs EG: Okadaic acid mimics the action of insulin in stimulating protein kinase activity in isolated adipocytes: the role of protein phosphatase 2A in attenuation of the signal. J Biol Chem 265: 16571–16580, 1990

    PubMed  Google Scholar 

  106. Ahn NG, Weiel JE, Chan CP, Krebs EG: Identification of multiple epidermal growth factor-stimulated protein serine/threonine kinases from Swiss 3T3 cells. J Biol Chem 265: 11487–11494, 1990

    PubMed  Google Scholar 

  107. Grande J, Perez M, Plana M, Itarte E: Acute effects of insulin and glucagon on hepatic casein kinase 2 in adult fed rats: correlation of the effects on casein kinase 2 with the changes in glycogen synthase activity. Arch Bioch Biophys 275: 478–485, 1989

    Google Scholar 

  108. Carroll D, Santoro N, Marshak DR: Regulating cell growth: casein kinase-II-dependent phosphorylation of nuclear oncoproteins. Cold Spring Harbor Symp Quant Biol 53: 91–95, 1988

    PubMed  Google Scholar 

  109. DeBenedette M, Snow EC: Induction and regulation of casein kinase II during B lymphocyte activation. J Immunol 147: 2839–2845, 1991

    PubMed  Google Scholar 

  110. Mulner-Lorillon O, Cormier P, Labbe J-C, Doree M, Poulhe R, Osborne H, Belle R: M-phase-specific cdc2 protein kinase phosphorylates the β subunit of casein kinase II and increase casein kinase II activity. Eur J Biochem 193: 529–534, 1990

    PubMed  Google Scholar 

  111. Sanghera JS, Charlton LA, Paddon HB, Pelech SL: Purification and characterization of echinoderm casein kinase II. Regulation by protein kinase C. Biochem J 283: 829–837, 1992

    PubMed  Google Scholar 

  112. Agostinis P, Goris J, Pinna LA, Merlevede W: Regulation of casein kinase 2 by phosphorylation/dephosphorylation. Biochem J 248: 785–789, 1987

    PubMed  Google Scholar 

  113. Litchfield DW, Lüscher B, Lozeman FJ, Eisenman RN, Krebs EG: Phosphorylation of casein kinase II by p34cdc2 in vitro and at mitosis. J Biol Chem 267: 14943–13951, 1992

    Google Scholar 

  114. Scott JD: Cyclic nucleotide-dependent protein kinases. Pharmac Ther 50: 123–145, 1991

    Google Scholar 

  115. Pines J, Hunter T: Human cyclins A and B1 are differentially located in the cell and undergo cell cycle-dependent nuclear transport. J Cell Biol 115: 1–17, 1991

    PubMed  Google Scholar 

  116. Glover CVC: A filamentous form of Drosophila casein kinase II. J Biol Chem 261: 14349–14354, 1986

    PubMed  Google Scholar 

  117. Serrano L, Hernandez MA, Diaz-Nido J, Avila J: Association of casein kinase II with microtubules. Exp Cell Res 181: 263–272, 1989

    PubMed  Google Scholar 

  118. Dougherty JJ, Rabideau DA, Iannotti AM, Sullivan WP, Toft DO: Identification of the 90 kDa substrate of the rat liver type II casein kinase with the heat shock protein which binds steroid receptors. Biochim Biophys Acta 927: 74–80, 1987.

    PubMed  Google Scholar 

  119. Miyata Y, Yahara I: The 90 kDa heat shock protein, HSP90, binds and protects casein kinase II from self-aggregation and enhances its kinase activity. J Biol Chem 267: 7042–7047, 1992

    PubMed  Google Scholar 

  120. Molina E, Pana M, Itarte E: Heterogeneity of rat liver cytosol casein kinase 2: association between the α/α′ subunits of casein kinase 2 and the phoshorylatable protein pp49. Biochem J 277: 811–818, 1991

    PubMed  Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Manitoba Institute of Cell Biology, University of Manitoba, 100 Olivia Street, R3E 0V9, Winnipeg, Manitoba, Canada

    David W. Litchfield

  2. Department of Biochemistry and Molecular Biology, University of Manitoba, R3E 0V9, Winnipeg, Manitoba, Canada

    David W. Litchfield

  3. Institut für Molekularbiologie, Medizinische Hochschule Hannover, D 3000, Hannover 1, Germany

    Bernard Lüscher

Authors
  1. David W. Litchfield
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Bernard Lüscher
    View author publications

    You can also search for this author in PubMed Google Scholar

Rights and permissions

Reprints and permissions

About this article

Cite this article

Litchfield, D.W., Lüscher, B. Casein kinase II in signal transduction and cell cycle regulation. Mol Cell Biochem 127, 187–199 (1993). https://doi.org/10.1007/BF01076770

Download citation

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF01076770

Key words

Search

Navigation