Type-2 casein kinases: General properties and substrate specificity

Peptides and Protein Phosphorylation

Volumn , Issue , 2018, Pages 145-169

  Pinna, Lorenzo A ^a   Meggio, Flavio ^a   Marchiori, Fernando ^a  

^a UNIVERSITY OF PADOVA   (Italy)

Author keywords

[No Author keywords available]

Indexed keywords

EID: 85053092400     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1201/9781351075442     Document Type: Chapter

References (159)

1. Burnett, G. and Kennedy, E. P., The enzymatic phosphorylation of proteins, J. Biol. Chem., 211, 969, 1954.
2. Rabinowitz, M. and Lipmann, F., Reversible phosphate transfer between yolk phosphoprotein and adenosine triphosphate, J. Biol. Chem., 235, 1043, 1960.
3. Krebs, E. G. and Fischer, E. H., The phosphorylase b to a converting enzyme of rabbit skeletal muscle, Biochim. Biophys. Acta, 20, 150, 1956.
4. Walsh, D. A., Perkins, J. P., and Krebs, E. G., An adenosine 3',5'-monophosphate dependent protein kinase from rabbit skeletal muscle, J. Biol. Chem., 243, 3763, 1968.
5. Rodnight, R. and Lavin, B. E., Phosvitin kinase from brain: activation by ions and subcellular distribution, Biochem. J., 93, 84, 1964.
6. Pinna, L. A., Baggio, B., Moret, V., and Siliprandi, N., Isolation and properties of a protein kinase from rat liver microsomes, Biochim. Biophys. Acta, 178, 199, 1969.
7. Takeda, M., Yamamura, H., and Ohga, Y., Phosphoprotein kinases associated with rat liver chromatin, Biochem. Biophys. Res. Commun., 42, 103, 1971.
8. Pinna, L. A., Donella, A., and Moret, V., Characterization of cytosol phosphopeptides, FEBS Lett., 37, 183, 1973.
9. Baggio, B., Pinna, L. A., Moret, V., and Siliprandi, N., A simple procedure for the purification of rat liver phosvitin kinase, Biochim. Biophys. Acta, 212, 515, 1970.
10. Pinna, L. A., Meggio, F., and Donella-Deana, A., Structure of the sites undergoing phosphorylation by protein kinases, with special reference to “casein kinases”, in Protein Phosphorylation and Bioregulation, Thomas, G., Podesta, E. G., and Gordon, J., Eds., S. Karger, Basel, 1980, 8.
11. Hathaway, G. M. and Traugh, J. A., Case in kinases: multipotential protein kinases, Curr. Top. Cell. Regul., 21, 101, 1982.
12. Cochet, C., Feige, J. J., Pirollet, F., Keramidas, M., and Chambaz, E. M., Selective inhibition of a cyclic nucleotide independent protein kinase (G type casein kinase) by quercetin and related polyphenols, Biochem. Pharmacol., 31, 1357, 1982.
13. Meggio, F., Donella-Deana, A., Brunati, A. M., and Pinna, L. A., Inhibition of rat liver cytosol casein kinases by heparin, FEBS Lett., 141, 257, 1982.
14. Meggio, F., Pinna, L. A., Marchiori, F., and Borin, G., Polyglutamyl peptides: a new class of inhibitors of type-2 casein kinases, FEBS Lett., 162, 235, 1983.
15. Meggio, F., Marchiori, F., Borin, G., Chessa, G., and Pinna, L. A., Synthetic peptides including acidic clusters as substrates and inhibitors of rat liver casein kinase TS (Type-2), J. Biol. Chem., 259, 14576, 1984.
16. Maenpaa, P. H., Effects of polyamines and polyanions on a cyclic nucleotide-independent protein kinase, Biochim. Biophys. Acta, 498, 294, 1977.
17. Cochet, C., Job, D., Pirollet, F., and Chambaz, E. M., Adenosine 3',5'-monophosphate-independent protein kinase activities in the bovine adrenal cortex cytosol, Endocrinology, 106, 750, 1980.
18. Hathaway, G. M. and Traugh, J. A., Interactions of polyamines and magnesium with casein kinase II, Arch. Biochem. Biophys., 233, 133, 1984.
19. Yamamoto, M., Criss, W. E., Yoshimi, T., Yamamura, H., and Nishizuka, Y., A hepatic soluble cyclic nucleotide-independent protein kinase. Stimulation by basic polypeptides,. J. Biol. Chem., 254, 5049, 1979.
20. Meggio, F., Brunati, A. M., and Pinna, L. A., Autophosphorylation of type-2 casein kinase-TS at both its a- and P-subunits, FEBS Lett., 160, 203, 1983.
21. Thornburg, W. and Lindell, T. J., Purification of rat liver nuclear protein kinase Nil, J. Biol. Chem., 252, 6660, 1977.
22. Cochet, C. and Chambaz, E. M., Oligomeric structure and catalytic activity of a G type casein kinase, J. Biol. Chem., 258, 1403, 1983.
23. Glover, C. V. C., Shelton, E. R., and Brutlag, D. L., Purification and characterization of a type II casein kinase from Drosophila melanogaster, J. Biol. Chem., 258, 3258, 1983.
24. Meggio, F. and Pinna, L. A., Subunit structure and autophosphorylation mechanism of casein kinase-TS (type-2) from rat liver cytosol, Eur. J. Biochem., 145, 593, 1984.
25. Dahmus, G. K., Glover, C. V. C., Brutlag, D. L., and Dahmus, M. E., Similarities in structure and function of calf thymus and Drosophila casein kinase II, J. Biol. Chem., 259, 9001, 1984.
26. Hathaway, G. M., Zoller, M. H., and Traugh, J. A., Identification of the catalytic subunit of casein kinase II by affinity labeling with 5'-p-fluorosulfonylbenzoyl adenosine, J. Biol. Chem., 256, 11442, 1981.
27. Feige, J.-J., Cochet, C., Pirollet, F., and Chambaz, E. M., Identification of the catalytic subunit of an oligomeric casein kinase (G type). Affinity labeling of the nucleotide site using 5'-p-(fluorosulfonyl)benzoyl adenosine, Biochemistry, 22, 1452, 1983.
28. Baydoun, H., Hoppe, J., Jacob, J., and Wagner, K. G., Purification and quaternary structure of a cyclic nucleotide-independent protein kinase (Nil) from porcine liver nuclei, FEBS Lett., 122, 231, 1980.
29. Delpech, M., Levy-Favatier, F., Moisand, F., and Kruh, J., Rat liver nuclear protein kinases N1 and Nil. Purification, subunit composition, substrate specificity, possible levels of regulation, Eur. J. Biochem., 160, 333, 1986.
30. Baydoun, H., Feth, F., Hoppe, J., Erdmann, H., and Wagner, K. G., The acidic peptide specific type II protein kinases from the nucleus and the cytosol of porcine liver are distinct, Arch. Biochem. Biophys., 245, 504, 1986.
31. Agostinis, P. and Pinna, L. A., unpublished data.
32. Meggio, F., Grankowski, N., Kudlicki, W., Szyszka, R., Gasior, E., and Pinna, L. A., Structure and properties of casein kinase-2 from Saccharomyces cerevisiae. A comparison with the liver enzyme, Eur. J. Biochem., 159, 31, 1986.
33. Ranart, M. F., Sastre, L., and Sebastian, J., Purification and properties of a cAMP-independent protein kinase from Dictyostelium discoideum, Eur. J. Biochem., 140, 47, 1984.
34. Padmanabha, R. and Glover, C. V. C., Casein kinase II of yeast contains two distinct polypeptides and an unusually large β-subunit, J. Biol. Chem., 262, 1829, 1987.
35. Erdmann, H., Bocher, M., and Wagner, K. G., Two protein kinases from nuclei of cultured tobacco cells with properties similar to the cyclic nucleotide-independent enzymes (NI and Nil) from animal tissue, FEBS Lett., 137, 245, 1982.
36. Erdmann, H., Bocher, M., and Wagner, K. G., The acidic peptide specific protein kinases from suspension cultured tobacco cells: a comparison of the enzymes from whole cells and isolated nuclei, Plant Sci., 41, 81, 1985.
37. Godwa, S. and Pillay, D. T. N., cAMP independent protein kinases from soybean cotyledons (Glicine max L.), Plant Sci. Lett., 25, 49, 1982.
38. Yan, T.-F. J. and Tao, M., Purification and characterization of a wheat germ protein kinase, J. Biol. Chem., 257, 7037, 1982.
39. Hathaway, G. M. and Traugh, J. A., Casein kinase II, Methods Enzymol., 99, 317, 1983.
40. Zandomeni, R. and Weinmann, R., Inhibitory effect of 5,6-dichloro-l-beta D-ribofuranosyl benzimidazole on a protein kinase, J. Biol. Chem., 259, 14804, 1984.
41. Hathaway, G. M. and Traugh, J. A., Kinetics of activation of casein kinase II by polyamines and reversal of 2,3-bisphosphoglycerate inhibition, J. Biol. Chem., 259, 7011, 1984.
42. Hathaway, G. M. and Traugh, J. A., Regulation of casein kinase II by 2,3-bisphosphoglycerate in erythroid cells, J. Biol. Chem., 259, 2850, 1984.
43. Glover, C. V. C., A filamentous form of Drosophila casein kinase II, J. Biol. Chem., 261, 14349, 1986.
44. Linnala-Kankkunen, A., Palvimo, J., and Maenpaa, P., Polyamines and heparin do not appreciably influence phosphorylation of chromatin proteins HMG 14 and HMG 17 by nuclear protein kinase II, Biochim. Biophys. Acta, 799, 122, 1984.
45. Ahmed, K., Goueli, S. A., and Williams-Ashman, H. G., Characteristics of polyamine stimulation of cyclic nucleotide-independent protein kinase reaction, Biochem. J., 232, 767, 1985.
46. Dougherty, J. J., Rabideau, D. A., Iannotti, A. M., Sullivan, W. P., and Toft, D. O., Identification of the 90 kDa substrate of rat liver type II casein kinase with the heat shock protein which binds steroid receptors, Biochim. Biophys. Acta, 921, 74, 1987.
47. Meggio, F., Agostinis, P., and Pinna, L. A., Casein kinases and their protein substrates in rat liver cytosol: evidence for their participation in multimolecular systems, Biochim. Biophys. Acta, 846, 248, 1985.
48. 2+ antagonized phosphorylation of calmodulin by casein kinase-2 and a spleen tyrosine protein kinase, FEBS Lett., 215, 261, 1987.
49. Bar-Zvi, D. and Branton, D., Clathrin-coated vesicles contain two protein kinase activities. Phosphorylation of clathrin p light chain by casein kinase II, J. Biol. Chem., 261, 9614, 1986.
50. Pirollet, F., Feige, J.-J., Cochet, C., Job, D., and Chambaz, E. M., Identification of a specific endogenous inhibitor of casein kinase (G type) in bovine adrenal cortex as a glycosaminoglycan mixture, Biochem. Biophys. Res. Commun., 100, 613, 1981.
51. Levy-Favatier, F., Delpech, M., Riffe, A., and Kruh, J., A 25,000 Dalton inhibitor of cAMP independent protein kinases present in rat liver HMG protein preparations, Biochem. Biophys. Res. Commun., 130, 149, 1985.
52. Tijssen, J. P. F., Dubbleman, T. M. A. R., and Van Steveninck, J., Isolation and characterization of polyphosphates from the yeast cell surface, Biochim. Biophys. Acta, 760, 143, 1983.
53. Offenbacher, S. and Kline, E. S., Evidence for polyphosphate in phosphorylated non-histone nuclear proteins, Arch. Biochem. Biophys., 231, 114, 1984.
54. Qi, S.-L., Yukioka, M., Morisawa, S., and Inoue, A., Heterogeneity of protein kinase Nil multiple subunit-polypeptides, FEBS Lett., 203, 104, 1986.
55. Agostinis, P., Goris, J., Pinna, L. A., and Merlevede, W., Regulation of casein kinase-2 by phosphor-ylation-dephosphorylation, Biochem. J., 248, 785, 1987.
56. Traugh, J. A., Tahara, S. M., Sharp, S. B., Safer, B., and Merrick, W. C., Factors involved in initiation of haemoglobin synthesis can be phosphorylated in vitro, Nature (London), 263, 163, 1976.
57. Issinger, O.-G., Benne, R., Hershey, J. W. B., and Trout, R. R., Phosphorylation in vitro of eukariotic initiation factors IF-E2 and IF-E3 by protein kinases, J. Biol. Chem., 251, 6471, 1976.
58. Fairbanks, G., Avruch, J., Dino, J. E., and Patel, V. P., Phosphorylation and dephosphorylation of spectrin, J. Supramol. Struct., 9, 97, 1978.
59. De Paoli-Roach, A. A., Roach, P. J., and Lamer, J., Multiple phosphorylation of rabbit skeletal muscle glycogen synthase, J. Biol. Chem., 254, 12062, 1979.
60. Hathaway, G. M., Lundak, T. S., Tahara, S. M., and Traugh, J. A., Isolation of protein kinases from reticulocytes and phosphorylation of initiation factors, Methods Enzymol., 60, 495, 1979.
61. Inoue, A., Tei, Y., Hasuma, T., Yukioka, M., and Morisawa, S., Phosphorylation of HMG 17 by protein kinase Nil from rat liver cell nuclei, FEBS Lett., 117, 68, 1980.
62. Dahmus, M. E., Phosphorylation of eukariotic DNA-dependent RNA polymerase, J. Biol. Chem., 256, 3332, 1981.
63. 07) able to phosphorylate glycogen synthase and phosvitin, J. Biol. Chem., 256, 8955, 1981.
64. Meggio, F., Donella-Deana, A., and Pinna, L. A., Endogenous phosphate acceptor proteins for rat liver cytosolic casein kinases, J. Biol. Chem., 256, 11958, 1981.
65. Pinna, L. A., Meggio, F., and Dediukina, M., Phosphorylation of troponin-T by casein kinase TS, Biochem. Biophys. Res. Commun., 100, 449, 1981.
66. Villar-Palasi, C. and Kumon, A., Purification and properties of a dog cardiac troponin-t kinase, J. Biol. Chem., 256, 7409, 1981.
67. Carmichael, D. F., Geahlen, R. L., Allen, S. M., and Krebs, E. G., Type II regulatory subunit of cAMP-dependent protein kinase. Phosphorylation by casein kinase II at a site that is also phosphorylated in vivo, J. Biol. Chem., 257, 10440, 1982.
68. Hemmings, B. A., Aitken, A., Cohen, P., Rymond, M., and Hofmann, F., Phosphorylation of the type II regulatory subunit of cAMP-dependent protein kinase by glycogen synthase kinase 3 and glycogen synthase kinase 5, Eur. J. Biochem., 127, 473, 1982.
69. Yan, T.-F. and Tao, M., Studies on an endogenous substrate of wheat germ protein kinase, J. Biol. Chem., 257, 7044, 1982.
70. Walton, G. M. and Gill, G. N., Identity of the in vivo phosphorylation site in high mobility group 14 protein in HeLa cells with the site phosphorylated by casein kinase II in vitro, J. Biol. Chem., 258, 4440, 1983.
71. Tipper, J. P., Bacon, G. W., and Witters, L. A., Phosphorylation of acetyl-coenzyme A carboxylase by casein kinase I and casein kinase II, Arch. Biochem. Biophys., 227, 386, 1983.
72. Matsumura, S., Murakami, N., Tashiro, Y., Yasuda, S., and Kumon, A., Identification of calcium-independent myosin kinase with casein kinase II, Arch. Biochem. Biophys., 227, 125, 1983.
73. Meggio, F., Flamigni, F., Caldarera, C. M., Guarnieri, C., and Pinna, L. A., Phosphorylation of rat heart ornithine decarboxylase by type-2 casein kinase, Biochem. Biophys. Res. Commun., 122, 997, 1984.
74. Holcomb, E. R. and Friedman, D. L., Phosphorylation of the c-proteins of HeLa cell hnRNP particles: involvement of a casein kinase-11 type enzyme, J. Biol. Chem., 259, 31, 1984.
75. Murakami, N., Matsumura, S., and Kumon, A., Purification and identification of myosin heavy chain kinase from bovine brain, J. Biochem. (Tokyo), 95, 651, 1984.
76. Goueli, S. A., Holtzman, J. L., and Ahmed, K., Phosphorylation of the androgen receptor by a nuclear cAMP-independent protein kinase, Biochem. Biophys. Res. Commun., 123, 778, 1984.
77. Ackerman, P., Glover, C. V. C., and Osheroff, N., Phosphorylation of DNA topoisomerase II by casein kinase II: modulation of eukaryotic topoisomerase II activity in vitro, Proc. Natl. Acad. Sci. U.S.A., 82, 3164, 1985.
78. Durban, E., Doodenough, M., Mills, J., and Bush, H., Topoisomerase I phosphorylation in vitro and in rapidly growing Novikoff hepatoma cells, EMBO J., 4, 2921, 1985.
79. Goueli, S. A., Davis, A. T., Hiipakka, R. A., Liao, S., and Ahmed, K., Polyamine stimulated phosphorylation of prostatic spermine-binding protein is mediated only by cAMP-independent protein kinase, Biochem. J., 230, 293, 1985.
80. Clari, G. and Moret, V., Phosphorylation of membrane proteins by cytosolic casein kinases in human erythrocytes. Effect of monovalent ions, 2,3-bisphosphoglycerate and spermine, Mol. Cell. Biochem., 68, 181, 1985.
81. Chan, P.-K., Aldrich, M., Cook, R. G., and Busch, H., Amino acid sequence of protein B23 phosphorylation site, J. Biol. Chem., 261, 1868, 1986.
82. Mamrack, M. D., Olson, M. O. J., and Bush, H., Amino acid sequence and sites of phosphorylation in a highly acidic region of nucleolar nonhistone protein C23, Biochemistry, 18, 3381, 1979.
83. Guash, M. D., Plana, M., Pena, J. M., and Itarte, E., Phosphorylation of fibrinogen by casein kinase 2, Biochem. J., 234, 523, 1986.
84. Kishimoto, A., Brown, M. S., Slaughter, C. A., and Goldstein, J. L., Phosphorylation of serine 833 in cytoplasmic domain of low density lipoprotein receptor by a high molecular weight enzyme resembling casein kinase II, J. Biol. Chem., 262, 1344, 1987.
85. Donato, N. J., Ware, C. F., and Byus, C. V., A rat monoclonal antibody which interacts with mammalian ornithine decarboxylase at an epitope involved in phosphorylation, Biochim. Biophys. Acta, 884, 370, 1986.
86. Picton, C., Woodgett, J., Hemmings, B., and Cohen, P., Multisite phosphorylation of glycogen synthase from rabbit skeletal muscle. Phosphorylation of site 5 by glycogen synthase kinase-5 (casein kinase II) is a prerequisite for phosphorylation of site 3 by glycogen synthase kinase-3, FEBS Lett., 150, 191, 1982.
87. A/GSK-3 and casein kinase II, J. Biol. Chem., 259, 12144, 1984.
88. Ingebritsen, T. S. and Cohen, P., The protein phosphatases involved in cellular regulation. Classification and substrate specificities, Eur. J. Biochem., 132, 255, 1983.
89. Thoen, C., Van Hove, L., Cohen, P., and Siegers, H., Identification of protein phosphatases dephos-phorylating mRNP proteins from cryptobiotic gastrulae of the brine shrimp, A. salina, Biochem. Biophys. Res. Commun., 131, 84, 1985.
90. Agostinis, P., Goris, J., Vandenheede, J. R., Waelkens, E., Pinna, L. A., and Merlevede, W., Phosphorylation of the modulator protein of the ATP, Mg-dependent protein phosphatase by casein kinase TS. Reversal by PCS phosphatases and control by distinct phosphorylation site(s), FEBS Lett., 207, 167, 1986.
91. s2-casein by two rat liver “casein kinases”, FEBS Lett., 91, 216, 1978.
92. Pinna, L. A., Donella-Deana, A., and Meggio, F., Structural features determining the site specificity of a rat liver cAMP-independent protein kinase, Biochem. Biophys. Res. Commun., 87, 114, 1979.
93. Tuazon, P. T., Bingham, E., and Traugh, J. A., Cyclic nucleotide independent protein kinases from rabbit reticulocytes. Site-specific phosphorylation of casein variants, Eur. J. Biochem., 94, 497, 1979.
94. Donella-Deana, A., Meggio, F., and Pinna, L. A., Phosphorylation of threonine and serine residues of native and partially dephosphorylated caseins by a rat liver cAMP-insensitive protein kinase, Biochem. J., 179, 693, 1979.
95. Hoppe, J. and Baydoun, H., Substrate specificity of the nuclear protein kinase Nil from porcine liver. Studies with casein variants, Eur. J. Biochem., 117, 585, 1981.
96. Meggio, F., Donella-Deana, A., and Pinna, L. A., The use of soybean trypsin inhibitors as phosphor-ylatable substrates for a rat liver protein kinase, J. Biochem. (Tokyo), 86, 261, 1979.
97. Meggio, F., Donella-Deana, A., and Pinna, L. A., A study with model substrates of the structure of the sites phosphorylated by rat liver casein kinase TS, Biochim. Biophys. Acta, 662, 1, 1981.
98. Cohen, P., Yellowlees, D., Aitken, A., Donella-Deana, A., Hemmings, B. A., and Parker, P. J., Separation and characterisation of glycogen synthase kinase 3, glycogen synthase kinase 4 and glycogen synthase kinase 5 from skeletal muscle, Eur. J. Biochem., 124, 21, 1982.
99. Tashiro, Y., Matsumura, S., Murakami, N., and Kumon, A., The phosphorylation site for casein kinase II on 20,000 Da light chain of gizzard myosin, Arch. Biochem. Biophys., 233, 540, 1984.
100. Walton, G. M., Spiess, J., and Gill, G. N., Phosphorylation of high mobility group protein 14 by casein kinase II, J. Biol. Chem., 260, 4745, 1985.
101. Holmes, C. F. B., Kuret, J., Chisholm, A. K., and Cohen, P., Identification of the sites on skeletal muscle protein phosphatase inhibitor-2 phosphorylated by casein kinase II, Biochim. Biophys. Acta, 870, 408, 1986.
102. Meggio, F., Flamigni, F., Guarnieri, E., and Pinna, L. A., Location of the phosphorylation site for casein kinase-2 within the amino acid sequence of ornithine decarboxylase, Biochim. Biophys. Acta, 929, 116, 1987.
103. Chang, C., Salzman, A. G., Hiipakka, R. A., Huang, I.-Y., and Liao, S., Prostatic spermine binding protein. Cloning and nucleotide sequence of cDNA, aminoacid sequence and androgenic control of mRNA level, J. Biol. Chem., 262, 2826, 1987.
104. Byrne, B. M., van het Schip, A. D., van de Klundest, J. A. M., Arnberg, A. C., Gruber, M., and Ab, G., Aminoacid sequence of phosvitin derived from the nucleotide sequence of part of the chicken vitellogenin gene, Biochemistry, 23, 4275, 1984.
105. Pinna, L. A., Meggio, F., and Marchiori, F., unpublished data.
106. Pinna, L. A., Meggio, F., Marchiori, F., and Borin, G., Opposite and mutually incompatible structural requirements of type-2 casein kinase and cAMP-dependent protein kinase as visualized with synthetic peptide substrates, FEBS Lett., 171, 211, 1984.
107. Kuenzel, E. A. and Krebs, E. G., A synthetic peptide substrate specific for casein kinase II, Proc. Natl. Acad. Sci. U.S.A., 82, 737, 1985.
108. Marin, O., Meggio, F., Marchiori, F., Borin, G., and Pinna, L. A., Site specificity of casein kinase-2 (TS) from rat liver cytosol. A study with model peptide substrates, Eur. J. Biochem., 160, 239, 1986.
109. Pinna, L. A., Meggio, F., Marchiori, F., Perich, J. W., and Johns, R. B., unpublished data.
110. Chou, P. Y. and Fasman, G. D., Empirical prediction of protein conformations, Annu. Rev. Biochem., 47, 251, 1978.
111. Takio, K., Kuenzel, E. A., Walsh, K. A., and Krebs, E. G., Amino acid sequence of the p-subunit of bovine lung casein kinase II, Proc. Natl. Acad. Sci. U.S.A., 84, 4851, 1987.
112. Hunter, T. and Cooper, J. A., Protein-tyrosine kinases, Annu. Rev. Biochem., 54, 897, 1985.
113. Brunati, A. M., Marchiori, F., and Pinna, L. A., Isolation and partial characterization of distinct forms of tyrosine protein kinases from rat spleen, FEBS Lett., 88, 321, 1985.
114. Pinna, L. A., Meggio, F., Marchiori, F., and Brunati, A. M., unpublished data.
115. Pinna, L. A., Agostinis, P., and Ferrari, S., Selectivity of protein kinases and protein phosphatases: a comparative analysis, Adv. Protein Phosphatases, 3, 327, 1986.
116. Meggio, F., Chessa, G., Borin, G., Pinna, L. A., and Marchiori, F., Synthetic fragments of protamines as model substrates for rat liver cyclic AMP dependent protein kinase, Biochim. Biophys. Acta, 662, 94, 1981.
117. Purves, F., Donella-Deana, A., Marchiori, F., Leader, D. P., and Pinna, L. A., The substrate specificity of the protein kinase induced in cells infected with herpesviruses studies with synthetic substrates indicate structural requirements distinct from other protein kinases, Biochim. Biophys. Acta, 889, 208, 1986.
118. Meggio, F., Donella-Deana, A., and Pinna, L. A., Studies on the structural requirements of a microsomal cAMP-independent protein kinase, FEBS Lett., 106, 76, 1979.
119. Mercier, J. C., Phosphorylation of caseins, present evidence for an amino acid triplet code posttransla-tionally recognized by specific kinases, Biochimie, 63, 1, 1981.
120. Blomback, B., Blomback, M., Erdman, P., and Hessel, B., Amino acid sequence and the occurrence of phosphorus in human fibrinopeptides, Nature (London), 193, 883, 1962.
121. Tang, J., Sepulveda, P., Marciniszyn, J., Chen, K. C. S., Huang, W.-Y., Tao, N., Lin, D., and Lanier, J. P., Amino acid sequence of porcine pepsin, Proc. Natl. Acad. Sci. U.S.A., 70, 3437, 1973.
122. Henderson, J., Moir, A. J. G., Fothergill, L. A., and Fothergill, J. E., Sequences of sixteen phos-phoserine peptides from ovalbumins of eight species, Eur. J. Biochem., 114, 439, 1981.
123. Browne, C. A., Bennett, H. P. J., and Solomon, S., Isolation and characterization of corticotropin and melanotropin related peptides from the neurointermediary lobe of the rat pituitary by reversed-phase liquid chromatography, Biochemistry, 20, 4538, 1980.
124. Donella-Deana, A., Grankowski, N., Kudlicki, W., Szyska, R., Gasior, E., and Pinna, L. A., A type-1 casein kinase from yeast phosphorylates both serine and threonine residues of casein. Identification of the phosphorylation sites, Biochim. Biophys. Acta, 829, 180, 1985.
125. Ahmad, Z., Camici, M., DePaoli-Roach, A. A., and Roach, P. J., Glycogen synthase kinases. Classification of a rabbit liver casein and glycogen synthase kinase as a distinct enzyme, J. Biol. Chem., 259, 3420, 1984.
126. 2+-independent phosphorylation of tubulin and microtubule associated protein-2 by glycogen synthase (casein) kinase-1, Biochem. Biophys. Res. Commun., 121, 19, 1984.
127. Kuret, J., Woodgett, J. R., and Cohen, P., Multisite phosphorylation of glycogen synthase from rabbit skeletal muscle. Identification of the sites phosphorylated by casein kinase-1, Eur. J. Biochem., 151, 39, 1985.
128. Moore, A., Boulton, A. P., Heid, H. W., Jarasch, E. D., and Craig, R. K., Purification and tissue-specific expression of casein kinase from the lactating guinea-pig mammary gland, Eur. J. Biochem., 152, 729, 1985.
129. Pinna, L. A., Meggio, F., Marchiori, F., and Dobrowolska, G., unpublished data.
130. Saxena, A., Padmanabha, R., and Glover, C. V. C., Isolation and sequencing of cDNA clones encoding Alpha and Beta subunits of Drosophila melanogaster casein kinase II, Mol. Cell. Biol., 7, 3049, 1987.
131. Jakobi, R., Voss, H., and Pyorin, W., Human phosvitin casein kinase type II: molecular cloning and sequencing of full length cDNA encoding subunit beta, Eur. J. Biochem., in press, 1989.
132. Pfaff, M. and Anderer, F. A., Casein kinase II accumulation in the nucleolus and its role in nucleolar phosphorylation, Biochim. Biophys. Acta, 269, 100, 1988.
133. Grande, J., Perez, M., and Itarto, E., Phosphorylation of hepatic insulin receptor by casein kinase. II, FEBS Lett., 232, 130, 1988.
134. Jakubowicz, T. and Leader, D. P., A major phospho-protein of cells infected with pseudorabies virus is phosphorylated by cellular casein kinase II, J. Gen. Virol., 68, 1159, 1987.
135. Pisano, M., Hegazy, M. G., Reimann, E. M., and Dokas, L. A., Phosphorylation of protein B-50 (GAP-43) from adult rat brain cortex by casein kinase II, Biochem. Biophys. Res. Commun., 155, 1207, 1988.
136. Haugen-Scofield, J., Resing, K. A., and Dale, B. A., Characterization of an epidermal phosphatase specific for filaggrin phosphorylated by casein kinase II, J. Invest. Dermatol., 91, 553, 1988.
137. Koike, T. and Ohtsuki, K., Purification and characterization of a 400 kDa nonhistone chromatin protein that serves as an effective phosphate acceptor for casein kinase II from Ehrlich ascites tumor cells, J. Biochem. (Tokyo), 103, 928, 1988.
138. Levasseur, S., Poleck, T., Friedman, Y., and Burke, C., Purification of a 107 kDa casein kinase G substrate from thyroid cytosol, Mol. Cell. Biochem., 83, 157, 1988.
139. Issinger, O. G., Martin, T., Richter, W. W., Olson, M. and Fujiki, H., Hyperphosphorylation of N 60, a protein structurally and immunologically related to nucleolin, after tumor-promoter treatments, EMBO J., 7, 1621, 1988.
140. Brunati, A. M., Saggioro, D., Chieco-Bianchi, L., and Pinna, L. A., Altered protein kinase activities of lymphoid cells transformed by Abelson and Moloney leukemia viruses, FEBS Lett., 206, 59, 1986.
141. Scheider, H. R., Reichert, G. H., and Issinger, O. G., Enhanced casein kinase II activity during mouse embryogenesis. Identification of a 110 kDa phosphoprotein as the major phosphorylation product in mouse embryos and Krebs II mouse ascites tumor cells, Eur. J. Biochem., 161, 733, 1986.
142. Perez, M., Grande, J., and Itarte, E., Casein kinase 2 activity increases in the prereplicative phase of liver regeneration, FEBS Lett., 238, 273, 1988.
143. Durand, P., Vilgrain, J., Chambaz, E. M., and Saez, J. M., Changes in protein kinase activities in lamb adrenals at late gestation and early postnatal stages, Mol. Cell. Endocrinol., 53, 195, 1987.
144. Perez, M., Grande, J., and Itarte, E., Developmental changes in rat hepatic casein kinases 1 and 2, Eur. J. Biochem., 170, 493, 1987.
145. Sommercorn, J. and Krebs, E. G., Induction of casein kinase II during differentiation of 3T3-L1 cells, J. Biol. Chem., 262, 3839, 1987.
146. Mulner-Lorrilon, O., Marot, J., Cayla, X., Pouhle, R., and Belle, R., Purification and characterization of a casein kinase II-type enzyme from Xenopus laevis ovary. Biological effects on the meiotic cell division of full-grown oocyte, Eur. J. Biochem., 171, 107, 1988.
147. Mc Manaway, M. E., Eckberg, W. R., and Anderson, W. A., Characterization and hormonal regulation of casein kinase II activity in heterotransplanted human breast tumors in nude mice, Exp. Clin. Endocrinol., 90, 313, 1987.
148. Corvera, S., Roach, P. J., De Paoli-Roach, A. A., and Czech, M. P., Insulin action inhibits insulin like growth factor II (IGF-II) receptor phosphorylation in H-35 hepatoma cells. IGF-II receptors isolated from insulin treated cells exhibit enhanced in vitro phosphorylation by casein kinase II, J. Biol. Chem., 263, 3116, 1988.
149. Haystead, T. A., Campbell, D. G., and Hardie, D. G., Analysis of sites phosphorylated on acetyl-CoA carboxylase in response to insulin in isolated adipocytes. Comparison with sites phosphorylated by casein kinase 2 and the calmodulin-dependent multiprotein kinase, Eur. J. Biochem., 175, 347, 1988.
150. Klarlund, J. K. and Czech, M. P., Insulin like growth factor I and insulin rapidly increase casein kinase II activity in BALB/c 3T3 fibroblasts, J. Biol. Chem., 263, 15872, 1988.
151. Czech, M. P., Klarlund, J. K., Yagaloff, K. A., Bradford, A. P., and Lewis, R. E., Insulin receptor signaling activation of multiple serine kinases, J. Biol. Chem., 263, 11017, 1988.
152. Marchiori, F., Meggio, F., Marin, O., Borin, G., Calderan, A., Ruzza, P., and Pinna, L. A., Synthetic peptide substrates for casein kinase 2. Assessment of minimum structural requirements for phosphorylation, Biochim. Biophys. Acta, 971, 332, 1988.
153. Clark, S. J., Colthrust, D. R., and Proud, C. G., Structure and phosphorylation of eukariotic initiation factor 2. Casein kinase 2 and protein kinase C phosphorylates distinct but adjacent sites in the β-subunit, Biochim. Biophys. Acta, 968, 211, 1988.
154. Meggio, F., Boulton, A. P., Marchiori, F., Borin, G., Lennon, D. P. W., Calderan, A., and Pinna, L. A., Substrate-specificity determinants for a membrane bound casein kinase of lactating mammary gland. A study with synthetic peptides, Eur. J. Biochem., 177, 281, 1988.
155. Kuenzel, E. A., Mulligan, J. A., Sommercorn, J., and Krebs, E. G., Substrate specificity determinants for casein kinase II as deduced from studies with synthetic peptides, J. Biol. Chem., 262, 9136, 1987.
156. Meggio, F. and Pinna, L. A., Phosphorylation of phosvitin by casein kinase 2 provides the evidence that phosphoserines can replace carboxylic amino acids as specificity determinants, Biochim. Biophys. Acta, 971, 227, 1988.
157. Meggio, F., Perich, J. W., Johns, R. B., and Pinna, L. A., Partially dephosphorylated phosphopeptide AcSer(P)-Ser(P)-Ser(P) is an excellent substrate for casein kinase 2, FEBS Lett., 237, 225, 1988.
158. Fiol, C. J., Mahrenholz, A. M., Wang, Y., Roeske, R. W., and Roach, P. J., Formation of protein kinase recognition sites by covalent modification of the substrate. Molecular mechanism for the synergistic action of casein kinase II and glycogen synthase kinase 3, J. Biol. Chem., 262, 14042, 1987.
159. Dobrowolska, G., Meggio, F., Marchiori, F., and Pinna, L. A., Specificity determinants of Maize casein kinase IIB are related to but distinct from those of rat liver casein kinase II, Biochim. Biophys. Acta, 1010, 274, 1989.