Extraordinary pleiotropy of protein kinase CK2 revealed by weblogo phosphoproteome analysis

Biochimica et Biophysica Acta - Molecular Cell Research

Volumn 1793, Issue 5, 2009, Pages 847-859

  Salvi, Mauro ^a   Sarno, Stefania ^a,b   Cesaro, Luca ^a   Nakamura, Hideji ^c   Pinna, Lorenzo A ^a,b  

^a UNIVERSITY OF PADOVA   (Italy)

^b VENETIAN INSTITUTE OF MOLECULAR MEDICINE   (Italy)

^c HYOGO COLLEGE OF MEDICINE   (Japan)

Author keywords

ANTXR1; Bnip3L; EpsinR; HDGF; OSR1; Protein kinase CK2

Indexed keywords

ANTHRAX TOXIN; CASEIN KINASE II; EPSIN; HEPATOMA DERIVED GROWTH FACTOR; PROTEIN BNIP3; SERINE; THREONINE;

AMINO ACID SEQUENCE; ARTICLE; CONTROLLED STUDY; DATA BASE; HUMAN; HUMAN CELL; IN VITRO STUDY; OXIDATIVE STRESS; PLEIOTROPY; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN MOTIF; PROTEIN PHOSPHORYLATION; PROTEIN TARGETING; RESIDUE ANALYSIS; SEQUENCE ANALYSIS; VALIDATION PROCESS;

ADAPTOR PROTEINS, VESICULAR TRANSPORT; AMINO ACID SEQUENCE; ANIMALS; CASEIN KINASE II; CELL LINE; HUMANS; ISOENZYMES; MEMBRANE PROTEINS; MOLECULAR SEQUENCE DATA; PHOSPHOPROTEINS; PROTEIN-SERINE-THREONINE KINASES; PROTEOME; PROTEOMICS; PROTO-ONCOGENE PROTEINS; RECEPTORS, CELL SURFACE; RECOMBINANT FUSION PROTEINS; SEQUENCE ALIGNMENT; TUMOR SUPPRESSOR PROTEINS;

EID: 67349211782     PISSN: 01674889     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2009.01.013     Document Type: Article

References (42)

1. Villén J., Beausoleil S.A., Gerber S.A., and Gygi S.P. Large-scale phosphorylation analysis of mouse liver. Proc. Natl. Acad. Sci. U. S. A. 104 (2007) 1488-1493
2. Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., and Mann M. Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell 127 (2006) 635-648
3. Manning G., Whyte D.B., Martinez R., Hunter T., and Sudarsanam S. The protein kinase complement of the human genome. Science 298 (2002) 1912-1934
4. Pinna L.A., and Ruzzene M. How do protein kinases recognize their substrates?. Biochim. Biophys. Acta 1314 (1996) 191-225
5. Ubersax J.A., and Ferrel Jr. J.E. Mechanisms of specificity in protein phosphorylation. Nat. Rev., Mol. Cell Biol. 8 (2007) 530-541
6. Pagano M.A., Cesaro L., Meggio F., and Pinna L.A. Protein kinase CK2: a newcomer in the 'druggable kinome'. Biochem. Soc. Trans. 34 (2006) 1303-1306
7. Meggio F., and Pinna L.A. One-thousand-and-one substrates of protein kinase CK2?. FASEB J. 17 (2003) 349-368
8. Ahmed K., Gerber D.A., and Cochet C. Joining the cell survival squad: an emerging role for protein kinase CK2. Trends Cell Biol. 12 (2002) 226-230
9. Pinna L.A. The Raison D'Être of constitutively active protein kinases: the lesson of CK2. Acc. Chem. Res. 36 (2003) 378-384
10. Duncan J.S., and Litchfield D.W. Too much of a good thing: the role of protein kinase CK2 in tumorigenesis and prospects for therapeutic inhibition of CK2. Biochim. Biophys. Acta 1784 (2008) 33-47
11. Ahmad K.A., Wang G., Unger G., Slaton J., and Ahmed K. Protein kinase CK2 - a key suppressor of apoptosis. Adv. Enzyme Regul. 48 (2008) 179-187
12. Guerra B., and Issinger O.G. Protein kinase CK2 in human diseases. Curr. Med. Chem. 15 (2008) 1870-1886
13. Sarno S., and Pinna L.A. Protein kinase CK2 as a druggable target. Mol Biosyst. 4 (2008) 889-894
14. Crooks G.E., Hon G., Chandonia J.M., and Brenner S.E. WebLogo: a sequence logo generator. Genome Res. 14 (2004) 1188-1190
15. Chen W., Yazicioglu M., and Cobb M.H. The E1B 19K/Bcl-2-binding protein Nip3 is a dimeric mitochondrial protein that activates apoptosis. J. Biol. Chem. 279 (2004) 11129-11136
16. Mills I., Praefcke G.J., Vallis Y., Peter B.J., Olesen L.E., Gallop J.L., Butler P.J., Evans P.R., and McMahon H.T. EpsinR: an AP1/clathrin interacting protein involved in vesicle trafficking. J. Cell Biol. 160 (2003) 213-222
17. Go M.Y., Kim S., Partridge A.W., Melnyk R.A., Rath A., Deber C.M., and Mogridge J. Self-association of the transmembrane domain of an anthrax toxin receptor. J. Mol. Biol. 360 (2006) 145-156
18. Papandreou I., Krishna C., Kaper F., Cai D., Giaccia A.J., and Denko N.C. Anoxia is necessary for tumor cell toxicity caused by a low-oxygen environment. Cancer Res. 65 (2005) 3171-3178
19. Kishima Y., Yamamoto H., Izumoto Y., Yoshida K., Enomoto H., Yamamoto M., Kuroda T., Ito H., Yoshizaki K., and Nakamura H. Hepatoma-derived growth factor stimulates cell growth after translocation to the nucleus by nuclear localization signals. J. Biol. Chem. 277 (2002) 10315-10322
20. Sarno S., Vaglio P., Meggio F., Issinger O.G., and Pinna L.A. Protein kinase CK2 mutants defective in substrate recognition. Purification and kinetic analysis. J. Biol. Chem. 271 (1996) 10595-10601
21. Hanahan D. Techniques for transformation of E. coli. In: Glover D.M. (Ed). DNA Cloning, A Practical Approach Vol. 1 (1985), IRL Press, Oxford 109-135
22. Meggio F., Marin O., and Pinna L.A. Substrate specificity of protein kinase CK2. Cell. Mol. Biol. Res. 40 (1994) 401-409
23. Marin O., Meggio F., Draetta G., and Pinna L.A. The consensus sequences for cdc2 kinase and for casein kinase-2 are mutually incompatible. A study with peptides derived from the beta-subunit of casein kinase-2. FEBS Lett. 301 (1992) 111-114
24. 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 (1986) 239-244
25. Marin O., Meggio F., and Pinna L.A. Design and synthesis of two new peptide substrates for the specific and sensitive monitoring of casein kinases-1 and -2. Biochem. Biophys. Res. Commun. 198 (1994) 898-905
26. Diella F., Gould C.M., Chica C., Via A., and Gibson T.J. Phospho.ELM: a database of phosphorylation sites-update 2008. Nucleic Acids Res. 36 (2008) D240-244
27. Sarno S., Ghisellini P., Cesaro L., Battistutta R., and Pinna L.A. Generation of mutants of CK2alpha which are dependent on the beta-subunit for catalytic activity. Mol. Cell. Biochem. 227 (2001) 13-19
28. Poletto G., Vilardell J., Marin O., Pagano M.A., Cozza G., Sarno S., Falques A., Itarte E., Pinna L.A., and Meggio F. The regulatory beta subunit of protein kinase CK2 contributes to the recognition of the substrate consensus sequence. A study with an eIF2 beta-derived peptide. Biochemistry 47 (2008) 8317-8325
29. Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., and Gygi S.P. Phosphoproteomic analysis of the developing mouse brain. Mol. Cell. Proteomics 3 (2004) 1093-1101
30. Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., and Gygi S.P. Large-scale characterization of HeLa cell nuclear phosphoproteins. Proc. Natl. Acad. Sci. U. S. A. 101 (2004) 12130-12135
31. Vitari A.C., Deak M., Morrice N.A., and Alessi D.R. The WNK1 and WNK4 protein kinases that are mutated in Gordon's hypertension syndrome phosphorylate and activate SPAK and OSR1 protein kinases. Biochem. J. 391 (2005) 17-24
32. Moriguchi T., Urushiyama S., Hisamoto N., Iemura S., Uchida S., Natsume T., Matsumoto K., and Shibuya H. WNK1 regulates phosphorylation of cation-chloride-coupled cotransporters via the STE20-related kinases, SPAK and OSR1. J. Biol. Chem. 280 (2005) 42685-42693
33. Gagnon K.B., England R., and Delpire E. Characterization of SPAK and OSR1, regulatory kinases of the Na-K-2Cl cotransporter. Mol. Cell Biol. 26 (2006) 689-698
34. Taft S.C., and Weiss A.A. Toxicity of anthrax toxin is influenced by receptor expression. Clin. Vaccine Immunol. Clin. Vaccine Immunol. 15 (2008) 1330-1336
35. Okuda Y., Nakamura H., Yoshida K., Enomoto H., Uyama H., Hirotani T., Funamoto M., Ito H., Everett A.D., Hada T., and Kawase I. Hepatoma-derived growth factor induces tumorigenesis in vivo through both direct angiogenic activity and induction of vascular endothelial growth factor. Cancer Sci. 94 (2003) 1034-1041
36. Chen G., Ray R., Dubik D., Shi L., Cizeau J., Bleackley R.C., Saxena S., Gietz R.D., and Greenberg A.H. The E1B 19K/Bcl-2-binding protein Nip3 is a dimeric mitochondrial protein that activates apoptosis. J. Exp. Med. 186 (1997) 1975-1983
37. Mellor H.R., and Harris A.L. The role of the hypoxia-inducible BH3-only proteins BNIP3 and BNIP3L in cancer. Cancer Metastasis Rev. 26 (2007) 553-566
38. Sandoval H., Thiagarajan P., Dasgupta S.K., Schumacher A., Prchal J.T., Chen M., and Wang J. Essential role for Nix in autophagic maturation of erythroid cells. Nature 454 (2008) 232-235
39. Dai J., Jin W.H., Sheng Q.H., Shieh C.H., Wu J.R., and Zeng R. Protein phosphorylation and expression profiling by Yin-yang multidimensional liquid chromatography (Yin-yang MDLC) mass spectrometry. J. Proteome Res. 6 (2007) 250-262
40. Li X., Guan B., Srivastava M.K., Padmanabhan A., Hampton B.S., and Bieberich C.J. The reverse in-gel kinase assay to profile physiological kinase substrates. Nat. Methods 4 (2007) 957-962
41. Abouzied M.M., Baader S.L., Dietz F., Kappler J., Gieselmann V., and Franken S. Expression patterns and different subcellular localization of the growth factors HDGF (hepatoma-derived growth factor) and HRP-3 (HDGF-related protein-3) suggest functions in addition to their mitogenic activity. Biochem. J. 378 (2004) 169-176
42. Kubli D.A., Quinsay M.N., Huang C., Lee Y., and Gustafsson A.B. Bnip3 functions as a mitochondrial sensor of oxidative stress during myocardial ischemia and reperfusion. Am. J. Physiol. Heart Circ. Physiol. 295 (2008) H2025-H2031