One-thousand-and-one substrates of protein kinase CK2?

FASEB Journal

Volumn 17, Issue 3, 2003, Pages 349-368

  Meggio, Flavio ^a   Pinna, Lorenzo A ^a  

^a UNIVERSITY OF PADOVA   (Italy)

Author keywords

Casein kinase 2; CK2; Phosphoacceptor sites; Phosphoproteome

Indexed keywords

CASEIN KINASE II; DNA; PROTEIN KINASE; RNA; VIRUS PROTEIN;

ENZYME SUBSTRATE; HUMAN; NONHUMAN; PRIORITY JOURNAL; PROTEIN PHOSPHORYLATION; PROTEIN PROTEIN INTERACTION; REVIEW; RNA SYNTHESIS; TRANSCRIPTION REGULATION; VIRUS INFECTION; VIRUS REPLICATION;

AMINO ACIDS; ANIMALS; CASEIN KINASE II; PHOSPHORYLATION; PROTEIN-SERINE-THREONINE KINASES; PROTEOME; SUBSTRATE SPECIFICITY;

EUKARYOTA;

EID: 0037334895     PISSN: 08926638     EISSN: None     Source Type: Journal    
DOI: 10.1096/fj.02-0473rev     Document Type: Review

References (221)

1. Cohen, P. (2002) The origins of protein phosphorylation. Nat. Cell Biol. 4, E127-E130
2. Burnett, G., and Kennedy, E. P. (1954) The enzymatic phosphorylation of proteins. J. Biol. Chem. 211, 969-980
3. Kennedy, E. P. (1992) Sailing to Byzantium. Annu. Rev. Biochem. 61, 1-28
4. Pinna, L. A. (1994) A historical view of protein kinase CK2. Cell. Mol. Biol. Res. 383-390
5. Pinna, L. A. (2002) Protein kinase CK2: a challenge to canons. J. Cell Sci. 115, 3873-3878
6. Ghavidel, A., and Schultz, M. C. (2001) TATA binding protein-associated CK2 transduces DNA damage signals to the RNA polymerase III transcriptional machinery. Cell 106, 575-584
7. Guo, C., Yu, S., Davis, A. T., Wang, H., Green, J. E., and Ahmed, K. (2001) A potential role of nuclear matrix-associated protein kinase CK2 in protection against drug-induced apoptosis in cancer cells. J. Biol. Chem. 276, 5992-5999
8. Ahmed, K., Gerber, D. A., and Cochet, C. (2002) Joining the cell survival squad: an emerging role for protein kinase CK2. Trends Cell Biol. 12, 226-230
9. Tawfic, S., Yu, S., Wang, H., Faust, R., Davis, A., and Ahmed, K. (2001) Protein kinase CK2 in neoplasia. Histol. Histopathol. 16, 573-582
10. Pinna, L. A., Meggio, F., Donella-Deana, A., and Brunati, A. M. (1985) Type-2 casein kinases: structure, metabolic involvement and regulation. Proceedings of the 16th FEBS Congress, part A, pp. 153-163, VNU Science Press
11. Pinna, L. A. (1990) Casein kinase 2: an "eminence grise" in cellular regulation? Biochim. Biophys. Acta 1054, 267-284
12. Pinna, L. A., Meggio, F., and Sarno, S. (1995) Casein kinase-2 and cell signaling. In Biochemistry of Cell Membranes (S. Papa and J.M. Tager, eds.) pp. 15-27, Birkhäuser Verlag Basel, Switzerland.
13. Pinna, L. A., and Meggio, F. (1997) Protein kinase CK2 ("casein kinase-2") and its implication in cell division and proliferation. In Progress in Cell Cycle Res. (Meijer, L., Guidet, S., and Philippe, M., eds.) vol. 3, pp 77-97, Plenum Press, New York
14. Tuazon, P. T., and Traugh, J. A. (1991) Casein kinase I and II. Multipotential serine protein kinases: structure, function and regulation. In Advances in Second Messenger and Phosphoprotein Research (Greengard, P., and Robison, G. A., eds) Vol. 23, 123-164, Raven Press, Ltd., New York
15. Allende, J. E., and Allende, C. C. (1995) Protein kinase CK2: an enzyme with multiple substrates and a puzzling regulation. FASEB J. 9, 313-323
16. Guerra, B., and Issinger, O.-G. (1999) Protein kinase CK2 and its role in cellular proliferation, development and pathology. Electrophoresis 20, 391-408
17. Bergholtz, S., Andersen, T. O., Andersson, K. B., Borrebaek, J., Luescher, B., and Gabrielsen, S. (2001) The highly conserved DNA-binding domains of A-, B- and c-Myb differ with respect to DNA-binding, phosphorylation and redox properties. Nucleic Acids Res. 29, 3546-3456
18. Rohwer, A., Kittstein, W., Marks, F., and Gschwendt, M. (1999) Cloning, expression and characterization of an A6-related protein. Eur. J. Biochim. 263, 518-525
19. Minin, A. A., Zemskov, E. A., and Khaidarova, N. V. (1998) Protein kinase C and casein kinase 2 phosphorylate in vitro proteins of the annexin family from eggs of loach Misgurnus fossilis. Biochemistry 63, 1074-1077
20. Jaffe, L., Ryoo, H. D., and Mann, R. S. (1997) A role for phosphorylation by casein kinase II in modulating antennapedia activity in Drosophila. Genes Dev. 11, 1327-1340
21. Zhang, F., White, R. L., and Neufeld, K. L. (2001) Cell density and phosphorylation control the subcellular localization of adenomatous polyposis coli protein. Mol. Cell. Biol. 21, 8143-8156
22. Fritz, G., and Kaina, B. (1999) Phosphorylation of the DNA repair protein APE/REF-1 by CKII affects redox regulation of AP-1. Oncogene 18, 1033-1040
23. Walter, J., Schindzielorz, A., Hartung, B., and Haass, C. (2000) Phosphorylation of the beta-amyloid precursor protein at the cell surface by ectocasein kinases 1 and 2. J. Biol. Chem. 275, 23523-23529
24. Hsieh, H. L., Song, C. J., and Roux, S. J. (2000) Regulation of a recombinant pea nuclear apyrase by calmodulin and casein kinase II. Biochim. Biophys. Acta 1494, 248-255
25. Madrid, R., Le-Maout, S., Barrault, M. B., Janvier, K., Benichou, S., and Merot, J. (2001) Polarized trafficking and surface expression of the AQP4 water channel are coordinated by serial and regulated interactions with different clathrin adaptor complexes. EMBO J. 20, 7008-7021
26. Kim, Y. M., Barak, L. S., Caron, M. G., and Benovic, J. L. (2002) Regulation of arrestin-3 phosphorylation by casein kinase II. J. Biol. Chem. 277, 16837-16846
27. Wada, T., Takagi, T., Yamaguchi, Y., Kawase, H., Hiramoto, M., Ferdous, A., Takayama, M., Lee, K. A., Hurst, H. C., and Handa, H. (1996) Copurification of casein kinase II with transcription factor ATF/E4TF3. Nucleic Acid Res. 24, 876-884
28. Yamaguchi, Y., Wada, T., Suzuki, F., Takagi, T., Hasegawa, and Handa, H. (1998) Casein kinase II interacts with the bZIP domains of several transcription factors. Nucleic Acid Res. 26, 3854-3861
29. Schwemmle, M., De, B., Shi, L., Banerjee, A., and Lipkin, W. I. (1997) Borna disease virus P-protein is phosphorylated by protein kinase C epsilon and casein kinase II. J. Biol. Chem. 272, 21818-21823
30. Desagher, S., Osen-Sand, A., Montessuit, S., Magnenat, E., Vilbois, F., Hochmann, A., Journot, L., Antonsson, B., and Martinou, J. C. (2001) Phosphorylation of bid by casein kinases I and II regulates its cleavage by caspase 8. Mol. Cell 8, 601-611
31. Negro, A., Meggio, F., Bertoli, A., Battistutta, R., Sorgato, M. C., and Pinna, L. A. (2000) Susceptibility of the prion protein to enzymic phosphorylation. Biochem. Biophys. Res. Commun. 271, 337-341
32. McShan, G. D., and Wilson, V. G. (2000) Casein kinase II phosphorylates bovine papillomavirus type 1 E1 in vitro at a conserved motif. J. Gen. Virol. 81, 1995-2004
33. O'Brien, K. A., Lemke, S. J., Cocke, K. S., Rao, R. N., and Beckmann, R. P. (1999) Casein kinase 2 binds to and phosphorylates BRCA1. Biochem. Biophys. Res. Commun. 260, 658-664
34. Grein, S., and Pyerin, W. (1999) BTF3 is a potential new substrate of protein kinase CK2. Mol. Cell. Biochem. 191, 121-128
35. Ekdahl, K. N., and Nilsson, B. (1997) Phosphorylation of complement component C3 after synthesis in U937 cells by a putative protein kinase, casein kinase 2, which is regulated by CD11b: evidence that membrane-bound proteases preferentially cleave phosphorylated C3. Biochem. J. 328, 625-633
36. Paas, Y., Bohana-Kashtan, O., and Fishelson, Z. (1999) Phosphorylation of the complement component, C9, by an ectoprotein kinase of human leukemic cells. Immunopharmacology 42, 175-185
37. Janson, I. M., Ek, B., and Ek, P. (1997) Phosphorylation of CaBP1 and CaBP2 by protein kinase CK2. J. Biochem. 121, 112-117
38. Liu, Z. P., Galindo, R. L., and Wasserman, S. A. (1997) A role for CKII phosphorylation of the cactus PEST domain in dorsoventral patterning of the Drosophila embryo. Gen. Dev. 11, 3413-3422
39. Ou, W. J., Thomas, D. Y., Bell, A. W., and Bergeron, J. J. (1992) Casein kinase II phosphorylation of signal sequence receptor alpha and the associated membrane chaperone calnexin. J. Biol. Chem. 267, 23789-23796
40. Padmanabhan, S., Elias-Arnanz, M., Carpio, E., Aparicio, P., and Murillo, F. J. (2001) Domain architecture of a high mobility group A-type bacterial transcriptional factor. J. Biol. Chem. 276, 41566-41575
41. Song, D. H., Sussman, D. J., and Seldin, D. C. (2000) Endogenous protein kinase CK2 participates in Wnt signaling in mammary epithelial cells. J. Biol. Chem. 275, 23790-23797
42. Sugano, S., Andronis, C., Green, R. M., Wang, Z. Y., and Tobin, E. M. (1998) Protein kinase CK2 interacts with and phosphorylates the Arabidopsis circadian clock-associated 1 protein. Proc. Natl. Acad. Sci. USA 95, 11020-11025
43. Ganju, R. K., Shpektor, R. G., Brenner, D. G., and Shipp, M. A. (1996) CD10/neutral endopeptidase 24.11 is phosphorylated by casein kinase II and coassociates with other phosphoproteins including the lyn src-related kinase. Blood 88, 4159-4165
44. Ritter, M., Buechler, C., Kapinsky, M., and Schmitz, G. (2001) Interaction of CD163 with the regulatory subunit of casein kinase II (CKII) and dependence of CD163 signaling on CKII and protein kinase C. Eur. J. Immun. 31, 999-1009
45. Formby, B., and Stern, R. (1998) Phosphorylation stabilizes alternatively spliced CD44 mRNA transcripts in breast cancer cells: inhibition by antisense complementary to casein kinase II mRNA. Mol. Cell. Biochem. 187, 28-31
46. Raman, C., Kuo, A., Deshane, J., Litchfield, D. W., and Kimberly, R. P. (1998) Regulation of casein kinase 2 by direct interaction with cell surface receptor CD5. J. Biol. Chem. 273, 19183-19189
47. Russo, G. L., van-den-Bos, C., Sutton, A., Coccetti, P., Baroni, M. D., Alberghina, L., and Marshak, D. R. (2000) Phosphorylation of Cdc28 and regulation of cell size y the protein kinase CKII in Saccharomyces cerevisiae. Biochem. J. 351, 143-150
48. Block, K., Boyer, T. G., and Yew, T. R. (2001) Phosphorylation of the human ubiquitin-conjugating enzyme, CDC34, by casein kinase 2. J. Biol. Chem. 276, 41049-41058
49. Liu, Z., Huntley, C. C., De, B. P., Das, T., Banerjee, A. K., and Oglesbee, M. J. (1997) Phosphorylation of canine distemper virus P protein by protein kinase C-zeta and casein kinase II. Virology 232, 198-206
50. Kanekatsu, M., Saito, H., Motohashi, K., and Hisabori, T. (1998) The beta subunit of chloroplast ATP synthase (CF0CF1-ATPase) is phosphorylated by casein kinase II. Biochem. Mol. Biol. Int. 46, 99-105
51. Dobransky, T., Davis, W. L., Xiao, G. H., and Rylett, R. J. (2000) Expression, purification and characterization of recombinant human choline acetyltransferase: phosphorylation of the enzyme regulates catalytic activity. Biochem. J. 349, 141-151
52. Chattopadhyay, D., Raha, T., and Chattopadhyay, D. (1997) Single serine phosphorylation within the acidic domain of Chandipura virus P protein regulates the transcription in vitro. Virology 239, 11-19
53. Dahma, H., Gourlet, P., Vandermeers, A., Vandermeers-Piret, M. C., and Robberecht, P. (2001) Evidence that the chromogranin B fragment 368-417 extracted from a pheochromocytoma is phosphorylated. Peptides 22, 1491-1499
54. Litchfield, D. W., Lozeman, F. J., Cicirelli, M. F., Harrylock, M., Ericsson, R. L., Piening, C. J., and Krebs, E. G. (1991) 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
55. Ralet, M. C., Fouques, D., Leonil, J., Molle, D., and Meunier, J. C. (1999) Soybean beta-conglycinin alpha subunit is phosphorylated on two distinct serines by protein kinase CK2 in vitro. J. Protein Chem. 18, 315-323
56. Yin, X. Y., Jedrzejewski, P. T., and Jiang, J. X. (2000) Casein kinase II phosphorylates lens connexin 45.6 and is involved in its degradation. J. Biol. Chem. 275, 6850-6856
57. Jung, E. J., Kang, Y. S., and Kim, C. W. (1998) Multiple phosphorylation of chicken protein tyrosine phosphatase 1 and human protein tyrosine phosphatase 1B by casein kinase II and p60c-src in vitro. Biochem. Biophys. Res. Commun. 246, 238-242
58. Kasahara, H., and Izumo, S. (1999) Identification of the in vivo casein kinase II phosphorylation site within the homeodomain of the cardiac tissue-specifying homeobox gene product Csx/Nkx2.5. Mol. Cell. Biol. 19, 526-536
59. Klenova, E. M., Chernukhin, I. V., El-Kady, A., Lee, R. E., Pugacheva, E. M., Loukinov, D. I., Goodwin, G. H., Delgado, D., Filippova, G. N., Leon, J., Morse, H. C., Neiman, P. E., and Lobanenkov, V. V. (2001) Functional phosphorylation sites in the C-terminal region of the multivalent multifunctional transcriptional factor CTCF. Mol. Cell.Biol. 21, 2221-2234
60. Coqueret, O., Martin, N., Berube, G., Rabbat, M., Litchfield, D. W., and Nepveu, A. (1998) DNA binding by cut homeodomain proteins is down-modulated by casein kinase II. J. Biol. Chem. 273, 2561-2566
61. Schuster, N., Goetz, C., Faust, M., Schneider, E., Prowald, A., Jungbluth, A., and Montenarh, M. (2001) Wild-type p53 inhibits protein kinase CK2 activity. J. Cell. Biochem. 81, 172-181
62. Engemann, H., Heinzel, V., Page, G., Preuss, U., and Scheidtmann, K. H. (2002) DAP-like kinase interacts with the rat homolog of S. pombe CDC5 protein, a factor involved in pre-mRNA splicing and required for G(2)M phase transition. Nucleic Acid Res. 30, 1408-1417
63. Karki, S., Tokito, M. K., and Holtzbaur, E. L. F. (1997) Casein kinase II binds to and phosphorylates cytoplasmic dynein. J. Biol. Chem. 272, 5887-5891
64. Lickert, H., Bauer, A., Kemler, R., and Stappert, J. (2000) Casein kinase II phosphorylation of E-cadherin increases E-cadherin/beta-catenin interaction and strengthens cell-cell adhesion. J. Biol. Chem. 275, 5090-5095
65. Ouyang, L., Chen, X., and Bieker, J. J. (1998) Regulation of erythroid Kruppel-like factor (EHLF) transcriptional activity by phosphorylation of a protein kinase casein kinase II site within its interaction domain. J. Biol. Chem. 273, 23019-23025
66. Gelsthorpe, M., Pulumati, M., McCallum, C., Dang-Vu, K., and Tsubota, S. I. (1997) The putative cell cycle gene, enhancer of rudimentary, encodes a highly conserved protein found in plants and animals. Gene 186, 189-195
67. Jensen, H. H., Hjerrild, M., Guerra, B., Larsen, M. R., Hojrup, P., and Boldyreff, B. (2001) Phosphorylation of the Fas associated factor FAF1 by protein kinase CK2 and identification of serines 289 and 291 as the in vitro phosphorylation sites. Int. J. Biochem. Cell Biol. 33, 577-589
68. Steplewski, A., Ebel, W., Planey, S. L., Alnemri, E. S., Robertson, N. M., and Litwack, G. (2000) Phosphorylation of the insect immunophilin FKBP46 by the Spodoptera frugiperda homolog of casein kinase II. Gene 246, 169-178
69. Miyata, Y., Chambraud, B., Radanyl, C., Leclerc, J., Lebeau, M. C., Renoir, J. M., Shirai, R., Catelli, M. J., Yahara, I., and Baulieu, E. E. (1998) Phosphorylation of the immunosuppressant FK506-binding protein FKBP52 by casein kinase II: regulation of HSP90-binding activity of FKBP52. Proc. Natl. Acad. Sci. USA 94, 14500-14506
70. Wilson, L. K., Dhillon, N., Thorner, J., and Martin, G. S. (1997) Casein kinase II catalyzes tyrosine phosphorylation of the yeast nucleolar immunophilin Fpr3. J. Biol. Chem. 272, 12961-12967
71. Fischer, T., Elenko, E., Wan, L., Thomas, G., and Farquhar, M. G. (2000) Membrane-associated GAIP is a phosphoprotein and can be phosphorylated by clathrin-coated vesicles. Proc. Natl. Acad. Sci. USA 97, 4040-4045
72. Gulli, M.P., Faubladier, M., Sicard, H., and CaizerguesFerrer, M. (1997) Mitosis-specific phosphorylation of gar2, a fission yeast nucleolar protein structurally related to nucleolin. Chromosoma 105, 532-544
73. Shimoyama, Y., Ohtaka, H., Nagata, N., Munakata, H., Hayashi, N., and Ohtsuki, K. (1996) Physiological correlation between glycyrrhizin, glycyrrhizin-binding lipoxygenase and casein kinase II. FEBS Lett. 391, 238-242
74. Nuthall, H. N., Husain, J., McLarren, K. W., and Stifani, S. (2002) Role for Hes1-induced phosphorylation in Groucho-mediated transcriptional repression. Mol. Cell. Biol. 22, 389-399
75. Mendez, R., and de Haro, C. (1994) Casein kinase II is implicated in the regulation of heme-controlled translational inhibitor of reticulocyte lysates. J. Biol. Chem. 269, 6170-6176
76. Fish, K. N., Soderberg-Naucler, C., and Nelson, J. A. (1998) Steady-state plasma membrane expression of human cytomegalovirus gB is determined by the phosphorylation state of Ser(900). J. Virol. 72, 6457-6464
77. Pflum, M. K., Tong, J. K., Lane, W. S., and Schreiber, S. L. (2001) Histone deacetylase 1 phosphorylation promotes enzymatic activity and complex formation. J. Biol. Chem. 276, 47733-47741
78. Ohtsuki, K., Maekawa, T., Harada, S., Karino, A., Morikawa, Y., and Ito, M. (1998) Biochemical characterization of HIV-1 Rev as a potent activator of casein kinase II in vitro. FEBS Lett. 428, 235-240
79. Lazaro, J. B., Boretto, J., Selmi, B., Capony, J. P., and Canard, B. (2000) Phosphorylation of AZT-resistant human immunodeficiency virus type 1 reverse transcriptase by casein kinase II in vitro. Effects of inhibitor sensitivity. Biochem. Biophys. Res. Commun. 275, 26-32
80. Schwanbeck, R., Gymnopoulos, M., Petry, I., Piekielko, A., Szewczuk, Z., Heyduk, T., Zechel, K., and Wisniewski, J. R. (2001) Consecutive steps of phosphorylation affect conformation and DNA binding of the Chironomus high mobility group A protein. J. Biol. Chem. 276, 26012-26021
81. Stemmer, C., Schwander, A., Bauw, G., Fojan, P., and Grasser, K. D. (2002) Protein kinase CK2 differentially phosphorylates maize chromosomal high mobility group (HMGB) proteins modulating their stability and DNA interactions. J. Biol. Chem. 277, 1092-1098
82. Pancetti, F., Bosser, R., Krehan, A., Pyerin, W., Itarte, E., and Bachs, O. (1999) Heterogeneous nuclear ribonucleoprotein A2 interacts with protein kinase CK2. Biochem. Biophys. Res. Commun. 260, 17-22
83. Bosser, R., Faura, M., Serratosa, J., Renau-Piqueras, J., Pruschy, M., and Bachs, O. (1995) Phosphorylation of rat liver heterogeneous nuclear ribonucleoproteins A2 and C can be modulated by calmodulin. Mol. Cell. Biol. 15, 661-670
84. Fienberg, A. A., Nordstedt, C., Belting, H. G., Czernik, A. J., Nairn, A. C., Gandy, S., Greengard, P., and Ruddle, F. H. (1999) Phylogenetically conserved CK-II phosphorylation site of the murine homeodomain protein Hoxb-6. J. Exp. Zool. 285, 76-84
85. Yaron, Y., McAdara, J. K., Lynch, M., Hughes, E., and Gasson, J. C. (2001) Identification of novel functional regions important for the activity of HOXB7 in mammalian cells. J. Immunol. 166, 5058-5067
86. Ruzzene, M., Brunati, A. M., Sarno, S., Marin, O., Donella-Deana, A., and Pinna, L. A. (2000) Ser/Thr phosphorylation of hematopoietic specific protein 1 (HS1). Implication of protein kinase CK2. Eur. J. Biochem. 267, 3065-3072
87. Ford, H. L., Landesman-Bollag, E., Dacwag, C. S., Stukenberg, P. T., Pardee, A. B., and Seldin, D. C. (2000) Cell cycle-regulated phosphorylation of the human SIX1 homeodomain protein. J. Biol. Chem. 275, 22245-22254
88. Ng, T. I., Ogle, W. O., and Roizman, B. (1998) U (L) 13 protein kinase of herpes simplex virus 1 complexes with glycoprotein E and mediates the phosphorylation of the viral Fc receptor: glycoproteins E and I. Virology 241, 37-48
89. Conner, J. (1999) The unique N terminus of herpes simplex virus type 1 ribonucleotide reductase large subunit is phosphorylated by casein kinase 2, which may have a homologue in Escherichia coli. J. Gen. Virol. 80, 1471-1476
90. Mitchell, C., Blaho, J. A., McCormick, A. L., and Roizman, B. (1997) The nucleotidylylation of herpes simplex virus 1 regulatory protein alpha22 by human casein kinase II. J. Biol. Chem. 272, 25394-25400
91. Morrison, E. E., Wang, Y. F., and Meredith, D. M. (1998) Phosphorylation of structural components promotes dissociation of the herpes simplex virus type 1 tegument. J. Virol. 72, 7108-7114
92. O'Reilly, D., Hanscombe, O., and O'Hare, P. (1997) A single serine residue at position 375 of VP16 is critical for complex assembly with Oct-1 and HCF and is a target of phosphorylation by casein kinase II. EMBO J. 16, 2420-2430
93. Hardtke, C. S., Gohda, K., Osterlund, M. T., Oyama, T., Okada, K., and Deng, X. W. (2000) HY5 stability and activity in arabidopsis is regulated by phosphorylation in its COP1 binding domain. EMBO J. 19, 4997-5006
94. Wadd, S., Bryant, H., Filhol, O., Scott, J. E., Hsieh, T. Y., Everett, R. D., and Clements, J. B. (1999) The multifunctional herpes simplex virus IE63 protein interacts with heterogeneous ribonucleoprotein K and with casein kinase 2. J. Biol. Chem. 274, 28991-28998
95. Briggs, L. J., Johnstone, R. W., Elliot, R. M., Xiao, C. Y., Dawson, M., Trapani, J. A., and Jans, D. A. (2001) Novel properties of the protein kinase CK2-site-regulated nuclear localization sequence of the interferon-induced nuclear factor IFI16. Biochem. J. 353, 69-77
96. Hoeck, W. G., and Mukku, V. R. (1994) Identification of the major sites of phosphorylation in IGF binding protein-3. J. Cell. Biochem. 56, 262-273
97. Shen, J., Channavajhala, P., Seldin, D. C., and Sonenshein, G. E. (2001) Phosphorylation by the protein kinase CK2 promotes the calpain-mediated degradation of I kappa B alpha. J. Immunol. 167, 4919-4925
98. Chu, Z. L., McKinsey, T. A., Liu, L. L., Qi, X. X., and Ballard, D. W. (1996) Basal phosphorylation of the PEST domain in I kappa B beta regulates its functional interaction with the c-rel pro-oncogene product. Mol. Cell. Biol. 16, 5974-5984
99. Sanz-Ezquerro, J. J., Santaren, J. F., Sierra, T., Aragon, T., Ortega, J., Ortin, J., Smith, G. L., and Nieto, A. (1998) The PA influenza virus polymerase subunit is a phosphorylated protein. J. Gen. Virol. 79, 471-478
100. Lin, R. T., and Hiscott, J. (1999) A role for casein kinase II phosphorylation in the regulation of IRF-1 transcriptional activity. Mol. Cell. Biochem. 191, 169-180
101. Birnbaum, M. J., van Zundert, B., Vaughan, P. S., Whitmarsh, A. J., van Wijnen, A. J., Davis, R. J., Stein, G. S., and Stein, J. L. (1997) Phosphorylation of the oncogenic transcription factor interferon regulatory factor 2 (IRF2) in vitro and in vivo. J. Cell. Biochem. 66, 175-183
102. Carbonnet, F., Hattab, C., Cartron, J. P., and Bertrand, O. (1998) Kell and Kx, two disulfide linked proteins of the human erythrocyte membrane, are phosphorylated in vivo. Biochem. Biophys. Res. Commun. 247, 569-575
103. Macica, C. M., and Kaczmarek, L. K. (2001) Casein kinase-2 determines the voltage dependence of the Kv3.1 channel in auditory neurons and transfected cells. J. Neurosci. 21, 1160-1168
104. Wong, E. V., Schaefer, A. W., Landreth, G., and Lemmon, V. (1996) Casein kinase II phosphorylates the neural cell adhesion molecule L1. J. Neurochem. 66, 779-786
105. Park, J. W., and Bae, Y. S. (1999) Phosphorylation of ribosomal protein L5 by protein kinase CKII decreases its 5S rRNA binding activity. Biochem. Biophys. Res. Commun. 263, 475-481
106. Fan, H., Sakulich, A. L., Goodier, J. L., Zhang, X., Qin, J., and Maraia, R. J. (1997) Phosphorylation of the human La antigen on serine 366 can regulate recycling of RNA polymerase III transcription complexes. Cell 88, 707-815
107. Hatomi, M., Tanigawa, K., Fujihara, M., Ito, J., Yanahira, S., and Ohtsuki, K. (2000) Characterization of bovine and human lactoferrins as glycyrrhizin-binding proteins and their phosphorylation in vitro by casein kinase II. Biol. Pharm. Bull. 23, 1167-1172
108. Sugano, S., Andronis, C., Ong, M. S., Green, R. M., and Tobin, E. M. (1999) The protein kinase CK2 is involved in regulation of circadian rhythms in Arabidopsis. Proc. Natl. Acad. Sci. USA 96, 12362-12366
109. Sapir, T., Cahana, A., Seger, R., Nekhai, S., and Reiner, O. (1999) LIS1 is a microtubule-associated phosphoprotein. Eur. J. Biochem. 265, 181-188
110. Trott, R. L., Kalive, M., Paroush, Z., and Bidwai, A. P. (2001) Drosophila melanogaster casein kinase II interacts with and phosphorylates the basic helix-loop-helix proteins m5, m7 and m8 derived from the Enhancer of split complex. J. Biol. Chem. 276, 2159-2167
111. Lotfering, B., Muhlberger, E., Tamura, T., Klenk, H. D., and Becker, S. (1999) The nucleoprotein of Marburg virus is target for multiple cellular kinases. Virology 255, 50-62
112. Tsutsui, H., Geltinger, C., Murata, T., Itakura, K., Wada, T., Handa, H., and Yokoyama, K. K. (1999) The DNA-binding and transcriptional activities of MAZ, a myc-associated zinc finger protein are regulated by casein kinase II. Biochem. Biophys. Res. Commun. 262, 198-205
113. Malikova, M. A., Syomin, B. V., and Stepanov, A. S. (2001) Phosphorylation of the protein encoded by the first open reading frame of the MDG4 transposable element (gypsy) by homologous and heterologous casein kinases type 2. Biochemistry (Moscow) 66, 205-210
114. Glavy, J. S., Horwitz, S. B., and Orr, G. A. (1997) Identification of the in vivo phosphorylation sites for acidic-directed kinases in murine mdr1b P-glycoprotein. J. Biol. Chem. 272, 5909-5914
115. Rosorius, O., Issinger, O. G., and Braulke, T. (1993) Phosphorylation of the cytoplasmic tail of the 300-kDa mannose 6-phosphate receptor is required for the interaction with a cytosolic protein. J. Biol. Chem. 268, 21470-21473
116. Hemer, F., Korner, C., and Braulke, T. (1993) Phosphorylation of the human 46-kDa mannose 6-phosphate receptor in the cytoplasmic domain at serine 56. J. Biol. Chem. 268, 17108-17113
117. Komaba, S., Hamao, H., Murata-Hori, M., and Hosoya, H. (2001) Identification of myosin II kinase from sea urchin eggs as protein kinase CK2. Gene 275, 141-148
118. Rittschof, D., and, Traugh, J. A. (1982) Identification of casein kinase II and phosphorylated proteins associated with messenger ribonucleoproteins particles from reticulocytes. Eur. J. Biochem. 123, 333-336
119. Longshaw, V. M., Dirr, H. W., Blatch, G. L., and Lassle, M. (2000) The in vitro phosphorylation of the co-chaperone mSTI1 by cell cycle kinases substantiates a predicted casein kinase II-p34(cdc2)-NLS (CcN) motif. Biol. Chem. 381, 1133-1138
120. Ehrnsperger, C., and Volknandt, W. (2001) Major vault protein is a substrate of endogenous protein kinases in CHO and PC12 cells. Biol. Chem. 382, 1463-1471
121. Winter, B., Kautzner, I., Issinger, O.-G, and Arnold, H. H. (1998) Two putative protein kinase CK2 phosphorylation sites are important for Myf-5 activity. Biol. Chem. 378, 1445-1456
122. Li, M. F., Strand, D., Krehan, A., Pyerin, W., Heid, H., Neumann, B., and Mechler, B. M. (1999) Casein kinase 2 binds and phosphorylates the nucleosome assembly protein 1 (NAP1) in Drosophila melanogaster. J. Mol. Biol. 293, 1067-1084
123. Rodriguez, P., Pelletier, J., Price, G. B., and Zannis-Hadjopoulos, M. (2000) NAP-2: histone chaperone function and phosphorylation state through the cell cycle. J. Mol. Biol. 298, 225-238
124. Yamauchi, S., Tokita, Y., Aono, S., Matsui, F., Shuo, T., Ito, H., Kato, K., Kasahara, K., and Oohira, A. (2002) Phosphorylation of neuroglycan C, a brain-specific transmembrane chondroitin sulfate proteoglycan, and its localization in the lipid rafts. J. Biol. Chem. 277, 20583-20590
125. Dokas, L. A., Ting, S. M., Edgar, M. A. N., Oestreicher, A. B., Gispen, W. H., and DeGraan, P. N. E. (1998) Regulation of in vitro phosphorylation of the casein kinase II sites in B-50 (GAP-43). Brain Res. 781, 320-328
126. Porter, C. M., Havens, M. A., and Clipstone, N. A. (2000) Identification of amino acid residues and protein kinases involved in the regulation of NFATc subcellular localization. J. Biol. Chem. 275, 3543-3551
127. Wang, D., Westerheide, S. D., Hanson, J. L., and Baldwin, A. S. (2000) Tumor necrosis factor alpha-induced phosphorylation of RelA/p65 on Ser(529) is controlled by casein kinase II. J. Biol. Chem. 275, 32592-32597
128. Koike, T., and Ohtsuki, K. (1988) 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, 928-937
129. Liebermann, D. N., and Mody, I. (1999) Casein kinase II regulates NMDA channel function in hippocampal neuron. Nat. Neurosci. 2, 125-132
130. de Career, G., Cerdido, A., and Medina, F. J. (1997) NopA64, a novel nucleolar phosphoprotein from proliferating onion cells, sharing immunological determinants with mammalian nucleolin. Planta 201, 487-495
131. Meier, U. T., and Blobel, G. (1992) Nopp140 shuttles on tracks between nucleolus and cytoplasm. Cell 70, 127-138
132. Prieschl, E. E., Novotny, V., Csonga, R., Jaksche, D., ElbeBurger, A., Thumb, W., Auer, M., and Stingl, G. (1998) A novel splice variant of the transcription factor Nrf1 interacts with the TNF alpha promoter and stimulates transcription. Nucleic Acid Res. 26, 2291-2297
133. Kim, J., Lee, D., and Choe, J. (1999) Hepatitis C virus NS5A protein is phosphorylated by casein kinase II. Biochem. Biophys. Res. Commun. 257, 777-781
134. Eichwald, C., Vascotto, F., Fabbretti, E., and Burrone, O. R. (2002) Rotavirus NSP5: mapping phosphorylation sites and kinase activation and viriplasm localization domains. J. Virol. 76, 3461-3470
135. Cordenonsi, M., Turco, F., D'Atri, F., Hammar, E., Martinucci, G., Meggio, F., and Citi, S. (1999) Xenopus laevis occludin. Identification of in vitro phosphorylation sites by protein kinase CK2 and association with cingulin. Eur. J. Biochem. 264, 374-384
136. Pai, C. Y., Chen, H. K., Sheu, H. L., and Yeh, N. H. (1995) Cell-cycle-dependent alterations of a highly phosphorylated nucleolar protein p130 are associated with nucleologenesis. J. Cell Sci. 108, 1911-1920
137. Romero-Oliva, F., and Allende, J. E. (2001) Protein p21(WAF1/CIP1) is phosphorylated by protein kinase CK2 in vitro and interacts with the amino terminal end of the CK2 beta subunit. J. Cell. Biochem. 81, 445-452
138. Bryant, H. E., Matthews, D. A., Wadd, S., Scott, J. E., Kean, J., Graham, S., Russell, W. C., and Clements, J. B. (2000) Interaction between herpes simplex virus type 1 IE63 protein and cellular protein p32. J. Virol. 74, 11322-11328
139. Maekawa, T., Fujihara, M., and Ohtsuki, K. (2002) Characterization of human lactoferricin as a potent protein kinase CK2 activator regulated by A-kinase in vitro. Biol. Pharm. Bull. 22, 667-673
140. Park, H. S., Lee, S. M., Lee, J. H., Kim, Y. S., Bae, Y. S., and Park, J. W. (2001) Phosphorylation of the leucocyte NADPH oxidase subunit p47 (phox) by casein kinase 2: conformation-dependent phosphorylation and modulation of oxidase activity. Biochem. J. 358, 783-790
141. Plomann, M., Lange, R., Vopper, G., Cremer, H., Heinlein, U. A. O., Scheff, S., Baldwin, S. A., Leiges, M., Cramer, M., Paulsson, M., et al. (1998) Pacsin, a brain protein that is upregulated upon differentiation into neuronal cells. Eur. J. Biochem. 256, 201-211
142. Caldwell, B. D., Darlington, D. N., Penzes, P., Johnson, R. C., Eipper, B. A., and Mains, R. E. (1999) The novel kinase peptidylglycine alpha-amidating monooxygenase cytosolic interactor protein 2 interacts with the cytosolic routing determinants of the peptide processing enzyme peptidylglycine alpha-amidating monooxygenase. J. Biol. Chem. 274, 34646-34656
143. Kumar, B. R., Swaminathan, V., Banerjee, S., and Kundu, T. K. (2001) p300-mediated acetylation of human transcriptional coactivator PC4 is inhibited by phosphorylation. J. Biol. Chem. 276, 16804-16809
144. Tuteja, N., Beven, A. F., Shaw, P. J., and Tuteja, R. (2001) A pea homologue of human DNA helicase I is localized within the dense fibrillar component of the nucleolus and stimulated by phosphorylation with CK2 and cdc2 protein kinases. Plant J. 25, 9-17
145. Angenstein, F., Buchner, K., and Staak, S. (1999) Age-dependent differences in glutamate-induced phosphorylation systems in rat hippocampal slices. Hippocampus 9, 173-185
146. Han, M. H., Han, D. K. M., Aebersold, R. H., and Glomset, J. A. (2001) Effects of protein kinase CK2, extracellular signal-regulated kinase 2, and protein phosphatase 2A on a phosphatidic acid-preferring phospholipase A1. J. Biol. Chem. 276, 27698-27708
147. Veis, A., Wei, K. R., Sfeir, C., George, A., and Malone, J. (1998) Properties of the (DSS)n triplet repeat domain of rat dentin phosphophorin. Eur. J. Oral Sci. 106, Suppl. 1, 234-238
148. Hinchliffe, K. A., Ciruela, A., Letcher, A. J., Divecha, N., and Irvine, R. F. (1999) Regulation of type II alpha phosphatidylinositol phosphate kinase localization by the protein kinase CK2. Curr. Biol. 9, 983-986
149. Ganley, I. G., Walker, S. J., Manifava, M., Li, D. X., Brown, H. A., and Ktistakis, N. T. (2001) Interaction of phospholipase D1 with a casein-kinase-2-like serine kinase. Biochem. J. 354, 369-378
150. Pardo, P. S., Murray, P. F., Walz, K., Franco, L., and Passeron, S. (1998) In vivo and in vitro phosphorylation of the alpha 7/PRS1 subunit of Saccharomyces cerevisiae 20 S proteasome: in vitro phosphorylation by protein kinase CK2 is absolutely dependent on polylysine. Arch. Biochem. Biophys. 349, 397-401
151. Torres, J., and Pulido, R. (2001) The tumor suppressor PTEN is phosphorylated by the protein kinase CK2 at its C terminus. Implications for PTEN stability to proteasome-mediated degradation. J. Biol. Chem. 276, 993-998
152. Nambirajan, S., Radha, V., Kamatkar, S., and Swarup, G. (2000) PTP-S2, a nuclear tyrosine phosphatase, is phosphorylated and excluded from condensed chromosomes during mitosis. J. Biosci. 25, 33-40
153. Moyers, J. S., Zhu, J., and Kahn, C. R. (1998) Effects of phosphorylation on function of the Rad GTPase. Biochem. J. 333, 609-614
154. Kayukawa, K., Makino, Y., Yogosawa, S., and Tamura, T. (1999) A serine residue in the N-terminal acidic region of rat RPB6, one of the common subunits of RNA polymerases, is exclusively phosphorylated by casein kinase II in vitro. Gene 234, 139-147
155. Dupuy, L. C., Dobson, S., Bitko, V., and Barik, S. (1999) Casein kinase-2-mediated phosphorylation of respiratory syncytial virus phosphoprotein P is essential for the transcription elongation activity of the viral polymerase; phosphorylation by casein kinase 1 occurs mainly at Ser(215) and is without effect. J. Virol. 73, 8384-8392
156. Kohl, A., di Bartolo, V., and Bouloy, M. (1999) The Rift Valley fever virus nonstructural protein NSs is phosphorylated at serine residues located in casein kinase II consensus motifs in the carboxy-terminus. Virology 263, 517-525
157. Scotto, C., Mely, Y., Ohshima, H., Garin, J., Cochet, C., Chambaz, E., and Baudier, J. (1998) Cysteine oxidation in the mitogenic S100B protein leads to changes in phosphorylation by catalytic CKII-alpha subunit. J. Biol. Chem. 273, 3901-3908
158. Son, M. Y., Park, J. W., Kim, Y. S., Kang, S. W., Marshak, D. R., Park, W., and Bae, Y. S. (1999) Protein kinase CKII interacts with and phosphorylates the SAG protein containing Ring-H2 finger motif. Biochem. Biophys. Res. Commun. 263, 743-748
159. Fleming, Y., Armstrong, C. G., Morrice, N., Paterson, A., Goedert, M., and Cohen, P. (2000) Synergistic activation of stress-activated protein kinase 1/c-Jun N-terminal kinase (SAPK1/JNK) isoforms by mitogen-activated protein kinase kinase 4 (MKK4) and MKK7. Biochem. J. 352, 145-154
160. Plafker, S. M., Woods, A. S., and Gibson, W. (1999) Phosphorylation of simian cytomegalovirus assembly protein precursor (pAPNG.5) and proteinase precursor (pAPNG1): multiple attachment sites identified, including two adjacent serines in a casein kinase II consensus sequence. J. Virol. 73, 9053-9060
161. Milhon, J. L., Albert, T. J., Vande-Waa, E. A., O'Leary, K. A., Jackson, R. N., Kessler, M. A., Schuler, L. A., and Tracy, J. W. (2000) SmMAK16, the Schistosoma mansonii homologue of MAK16 from yeast, targets protein transport to the nucleolus. Mol. Biol. Parasitol. 108, 225-236
162. Zhou, Y. Y., Gross, W., Hong, S. H., and Privalsky, M. L. (2001) The SMRT corepressor is a target of phosphorylation by protein kinase CK2 (casein kinase II). Mol. Cell. Biochem. 220, 1-13
163. Armstrong, S. A., Barry, D. A., Leggett, R. W., and Mueller, C. R. (1997) Casein kinase II-mediated phosphorylation of the C terminus of sp1 decreases its Dna binding activity. J. Biol. Chem. 272, 13489-13495
164. Azuma, Y., Takio, K., Tabb, M. M., Vu, L., and Nomura, M. (1997) Phosphorylation of Srp1p, the yeast nuclear localization signal receptor, in vitro and in vivo. Biochimie 79, 247-259
165. Jellinek, D. A., Chang, A. C., Larsen, M. R., Wang, X., Robinson, P. J., and Reddel, R. R. (2000) Stanniocalcin 1 and 2 are secreted as phosphoproteins from human fibrosarcoma cells. Biochem. J. 350, 453-461
166. Foster, L. J., Yeung, B., Mohtashami, M., Ross, K., Trimble, W. S., and Klip, A. S. (1998) Binary interactions of the SNARE proteins syntaxin-4, SNAP23 and VAMP-2 and their regulation by phosphorylation. Biochemistry 37, 11089-11096
167. Okochi, M., Walter, J., Koyama, A., Nakajo, S., Baba, M., Iwatsubo, T., Meijer, L., Kahle, P. J., and Haas, C. (2000) Constitutive phosphorylation of the Parkinson's disease associated alpha-synuclein. J. Biol. Chem. 275, 390-397
168. Maldonado, E., and Allende, J. E. (1999) Phosphorylation of yeast TBP by protein kinase CK2 reduces its specific binding to DNA. FEBS Lett. 443, 256-260
169. Miravet, S., Piedra, J., Miro, F., Itarte, E., Garcia-de-Herreros, A., and Dunach, M. (2002) The transcriptional factor Tcf-4 contains different binding sites for beta-catenin and plakoglobin. J. Biol. Chem. 277, 1884-1891
170. Westmark, C. J., Ghose, R., and Huber, P. W. (2002) Phosphorylation of Xenopus transcription factor IIIA by an oocyte protein kinase CK2. Biochem. J. 362, 375-382
171. Ghavidel, A., and Schultz, M. C. (1997) Casein kinase II regulation of yeast TFIIIB is mediated by the TATA-binding protein. Genes Dev. 11, 2780-2789
172. Jones, N. C., Farlie, P. G., Minichiello, J., and Newgreen, D. F. (1999) Detection of an appropriate kinase activity in branchial arches I and II coincides with peak expression of the Treacher Collins syndrome gene product, treacle. Hum. Mol. Gen. 8, 2239-2245
173. Hanyaloglu, A. C., Vrecl, M., Kroeger, K. M., Miles, L. E. C., Quian, H. W., Thomas, W. G., and Eisne, K. A. (2001) Casein kinase II sites in the intracellular C-terminal domain of the thyrotropin-releasing hormone receptor and chimeric gonadotropin-releasing hormone receptors contribute to beta-arrestin dependent internalization. J. Biol. Chem. 276, 18066-18074
174. Meggio, F., Donella Deana, A., and Pinna, L. A. (1979) The use of soybean trypsin inhibitors as phosphorylatable substrates for a rat liver protein kinase. J. Biochem. (Tokyo) 86, 261-264
175. Semplici, F., Meggio, F., Pinna, L. A., and Oliviero, S. (2002) CK2-dependent phosphorylation of the E2 ubiquitin conjugating enzyme UBC3B induces its interaction with β-TRCP and enhances β-catenin degradation. Oncogene 21, 3978-3987
176. Seger, D., Gechtman, Z., and Shaltiel, S. (1998) Phosphorylation of vitronectin by casein kinase II. Identification of the sites and their promotion of cell adhesion and spreading. J. Biol. Chem. 273, 24805-24813
177. Krantz, D. E., Peter, D., Liu, Y. J., and Edwards, R. H. (1997) Phosphorylation of a vesicular monoamine transporter by casein kinase II. J. Biol. Chem. 272, 6752-6759
178. Chen, J. L., Das, T., and Banerjee, A. K. (1997) Phosphorylated states of vesicular stomatitis virus P protein in vitro and in vivo. Virology 228, 200-212
179. Klocke, B., and Knochel, W. (1995) Proteins of the Xenopus laevis zinc finger multigene family as targets for CK II phosphorylation. Mol. Cell. Biochem. 142, 49-59
180. Kalive, M., Trott, R. L., and Bidwai, A. P. (2001) A gene located at 71F in Drosophila melanogaster encodes a novel zinc-finger protein that interacts with protein kinase CK2. Mol. Cell. Biochem. 227, 99-105
181. Gavin, A. C., Bösche, M., Krause, R., Grandi, P., Marzloch, M., Bauer, A., Schultz, J., Rick, J. M., Michon, A.-M., Cruciat, C.-M., Remor, M., Höfert, C., Schelder, M., Brajenovic, M., Ruffner, H., Merino, A., Klein, K., Hudak, M., Dickson, D., Rudi, T., Gnau, V., Bauch, A., Bastuck, S., Huhse, B., Leutwein, C., Heurtler, M.-A., Copley, R. R., Edelmann, A., Querfurth, E., Rybin, V., Drewes, G., Ralda, M., Bouwmeester, T., Bork, P., Seraphin, B., Kuster, B., Neubauer, G., and Superti-Furga, G. (2002) Functional organization of the yeast proteome by systematic analysis of protein complexes. Nature (London) 415, 141-147
182. Massimi, P., Pim, D., Storey, A., and Banks, L. (1996) HPV-16 E7 and adenovirus E1a complex formation with TATA box binding protein is enhanced by casein kinase II phosphorylation. Oncogene 12, 2325-2330
183. Wang, Z., and Yang, Z. Q. (2000) Casein kinase II phosphorylation of caldesmon downregulates myosin-caldesmon interactions. Biochemistry 39, 11114-11120
184. Wong, H. N., Ward, M. A., Bell, A. W., Chevet, E., Bains, S., Blackstock, W. P., Solari, R., Thomas, D. Y., and Bergeron, J. J. (1998) Conserved in vivo phosphorylation of calnexin at casein kinase II sites as well as a protein kinase C/proline-directed kinase site. J. Biol. Chem. 273, 17227-17235
185. Saeki, K., You, A., and Takaku, F. (1999) Cell-cycle-regulated phosphorylation of cAMP response element-binding protein: identification of novel phosphorylation sites. Biochem. J. 338, 49-54
186. MacDonald, J. I., and Kent, C. (1994) Identification of phosphorylation sites in rat liver CTP: phosphocholine cytidylyltransferase. J. Biol. Chem. 269, 10529-10537
187. Rossi, R., Villa, A., Negri, C., Scovassi, I., Ciarrocchi, G., Biamonti, G., and Montecucco, A. (1999) The replication factory targeting sequence/PCNA-binding site is required in G(1) to control the phosphorylation status of DNA ligase I. EMBO J. 18, 5745-5754
188. Sheu, G. T., and Traugh, J. A. (1999) A structural model for elongation factor 1 (EF-1) and phosphorylation by protein kinase CKII. Mol. Cell. Biochem. 191, 181-186
189. Majumdar, R., Bandyopadhyay, A., Deng, H., and Maitra, U. (2002) Phosphorylation of mammalian translation initiation factor 5 (eIF5) in vitro and in vivo. Nucleic Acids Res. 30, 1154-1162
190. Kalafatis, M. (1998) Identification and partial characterization of factor Va heavy chain kinase from human platelets. J. Biol. Chem. 273, 8459-8466
191. Aroor, A. R., Denslow, N. D., Singh, L. P., O'Brien, T. W., and Wahba, A. J. (1994) Phosphorylation of rabbit reticulocyte guanine nucleotide exchange factor in vivo. Identification of putative casein kinase II phosphorylation sites. Biochemistry 33, 3350-3357
192. Schubert, U., Henklein, P., Boldyreff, B., Wingender, E., Strebel, K., and Porstmann, T. (1994) The human immunodeficiency virus type 1 encoded Vpu protein is phosphorylated by casein kinase-2 (CK-2) at positions Ser52 and Ser56 within a predicted alpha-helix-turn-alpha-helix-motif. J. Mol. Biol. 236, 16-25
193. Zhi, Y., and Sandri-Goldin, R. M. (1999) Analysis of the phosphorylation sites of herpes simplex virus type 1 regulatory protein ICP27. J. Virol. 73, 3246-3257
194. Taylor, J. A., Bren, G. D., Pennington, K. N., Trushin, S. A., Asin, S., and Paya, C. V. (1999) Serine 32 and serine 36 of IkappaBalpha are directly phosphorylated by protein kinase CKII in vitro. J. Mol. Biol. 290, 839-850
195. Hjerrild, M., Milne, D., Dumaz, N., Hay, T., Issinger, O. G., and Meek, D. (2001) Phosphorylation of murine double minute clone 2 (MDM2) protein at serine-267 by protein kinase CK2 in vitro and in cultured cells. Biochem. J. 355, 347-356
196. Korner, C., Herzog, A., Weber, B., Rosorius, O., Hemer, F., Schmidt, B., and Braulke, T. (1994) In vitro phosphorylation of the 46-kDa mannose 6-phosphate receptor by casein kinase II. Structural requirements for efficient phosphorylation. J. Biol. Chem. 269, 16529-16532
197. Vulsteke, V., Beullens, M., Waelkens, E., Stalmans, W., and Bollen, M. (1997) Properties and phosphorylation sites of baculovirus-expressed nuclear inhibitor of protein phosphatase-1 (NIPP-1). J. Biol. Chem. 272, 32972-32978
198. Murakami, N., Chauhan, V. P., and Elzinga, M. (1998) Two nonmuscle myosin II heavy chain isoforms expressed in rabbit brains: filament forming properties, the effects of phosphorylation by protein kinase C and casein kinase II, and location of the phosphorylation sites. Biochemistry 37, 1989-2003
199. Fadden, P., Haystead, T. A., and Lawrence, J. C., Jr. (1998) Phosphorylation of the translational regulator, PHAS-I, by protein kinase CK2. FEBS Lett. 435, 105-109
200. Rihs, H. P., Jans, D. A., Fan, H., and Peters, R. (1991) 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. EMBO J. 10, 633-639
201. Bennett, M. K., Miller, K. G., and Scheller, R. H. (1993) Casein kinase II phosphorylates the synaptic vesicle protein p65. J. Neurosci. 13, 1701-1707
202. Dubois, T., Kerai, P., Learmonth, M., Cronshaw, A., and Aitken, A. (2002) Identification of syntaxin-1A sites of phosphorylation by casein kinase I and casein kinase II. Eur. J. Biochem. 269, 909-914
203. Cardellini, E., Bramucci, M., Gianfranceschi, G. L., and Durban, E. (1994) Human topoisomerase I is phosphorylated in vitro on its amino terminal domain by protein kinase NII. Biol. Chem. Hoppe Seyler 375, 255-259
204. Escargueil, A. E., Plisov, S. Y., Filhol, O., Cochet, C., and Larsen, A. K. (2000) Mitotic phosphorylation of DNA topoisomerase II alpha by protein kinase CK2 creates the MPM-2 phosphoepitope on Ser-1469. J. Biol. Chem. 275, 34710-34718
205. Meggio, F., Marchiori, F., Borin, G., Chessa, G., and Pinna, L. A. (1984) Synthetic peptides including acidic clusters as substrates and inhibitors of rat liver casein kinase TS (Type-2). J. Biol. Chem. 259, 14576-14579
206. Marin, O., Meggio, F., Marchiori, F., Borin, G., and Pinna, L. A. (1986) Site specificity of casein kinase-2 (TS) from rat liver cytosol. A study with model peptide substrates. Eur. J. Biochem. 160, 239-244
207. Marin, O., Meggio, F., Draetta, G., and Pinna, L. A. (1992) The consensus sequences for cdc2 kinase and for casein kinase-2 are mutually incompatible. A study with peptides derived from the β-subunit of casein kinase-2. FEBS Lett. 301, 111-114
208. Songyang, Z., Lu, K. P., Kwon, Y. T., Tsai, L.-H., Filhol, O., Cochet, C., Brickey, D. A., Soderling, T. R., Bartleson, C., Graves, D. J., et al. (1996) A structural basis for substrate specificities of protein Ser/Thr kinases: primary sequence preference of casein kinase I and II, NIMA, Phosphorylase kinase, Calmodulin-dependent kinase II, CDK5 and Erk1. Mol. Cell. Biol. 16, 6486-6493
209. Roach, P. J. (1991) Multisite and hierarchal protein phosphorylation. J. Biol. Chem. 266, 14139-14142
210. Pinna, L. A., and Ruzzene, M. (1996) How do protein kinases recognize their substrates? Biochim. Biophys. Acta 1314, 191-225
211. Sarno, S., Vaglio, P., Marin, O., Issinger, O.-G., Ruffato, K., and Pinna, L. A. (1997) Mutational analysis of residues implicated in the interaction between protein kinase CK2 and peptide substrates. Biochemistry 36, 11717-11724
212. Niefind, K., Guerra, B., Ermakova, I., and Issinger, O.-G. (2001) Crystal structure of human protein kinase CK2: insights into basic properties of the CK2 holoenzyme. EMBO J. 20, 5320-5331
213. Marin, O., Sarno, S., Boschetti, M., Pagano, M. A., Meggio, F., Ciminale, V., D'Agostino, D. M., and Pinna, L. A. (2000) Unique features of HIV-1 Rev protein phosphorylation by protein kinase CK2 ("casein kinase-2"). FEBS Lett. 481, 63-67
214. Ficarro, S. B., McCleland, M. L., Stukenberg, P. T., Burke, D. J., Ross, M. M., Shabanowitz, J., Hunt, D. F., and White, F. M. (2002) Phosphoproteome analysis by mass spectrometry and its application to Saccharomyces cerevisiae. Nat. Biotechnol. 19, 301-305
215. Gerber, D. A., Souquere-Besse, S., Puvion, F., Dubois, M. F., Bensaude, O., and Cochet, C. (2000) Heat-induced relocalization of protein kinase CK2. Implication of CK2 in the context of cellular stress. J. Biol. Chem. 275, 23919-23919
216. Zetina, C. R. (2001) A conserved helix-unfolding motif in the naturally unfolded proteins. Proteins 44, 479-483
217. Steinmetz, M. O., Jahnke, W., Towbin, H., Garcia-Echeverria, C., Voshol, H., Müller, D., and van Oostrum, J. (2001) Phosphorylation disrupts the central helix in Op18/stathmin and suppresses binding to tubulin. EMBO Rep. 2, 505-510
218. Bucciantini, M., Giannoni, E., Chiti, F., Baroni, F., Formigli, L., Zurdo, J., Taddei, N., Ramponi, G., Dobson, C. M., and Stefani, M. (2002) Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases. Nature (London) 416, 507-511
219. Ruzzelle, M., Penzo, D., and Pinna, L. A. (2002) Protein kinase CK2 inhibitor 4,5,6,7-tetrabromobenzotriazole (TBB) induces apoptosis and caspase-dependent degradation of hematopoietic lineage cell-specific protein 1 (HS1) in Jurkat cells. Biochem. J. 364, 41-47
220. Pawson, T., and Scott, J. D. (1997) Signaling through scaffold, anchoring, and adaptor proteins. Science 278, 2075-2080
221. Yaffe, M. B., and Elia, A. E. H. (2001) Phosphoserine/phosphothreonine-binding domains. Curr. Opin. Cell Biol. 13, 131-138