A multifunctional network of basic residues confers unique properties to protein kinase CK2

Molecular and Cellular Biochemistry

Volumn 191, Issue 1-2, 1999, Pages 13-19

  Sarno, Stefania ^a   Vaglio, Philippe ^a   Cesaro, Luca ^a   Marin, Oriano ^a,b   Pinna, Lorenzo A ^a,c  

^a UNIVERSITY OF PADOVA   (Italy)

^b Biotechnology Center   (Italy)

^c Dipartimento di Chimica Biologica   (Italy)

Author keywords

Casein kinase 2; Heparin; Phospoacceptor peptides; Protein kinase CK2; Substrate recognition

Indexed keywords

CASEIN KINASE II; HEPARIN;

AMINO ACID SEQUENCE; ARTICLE; BETA CHAIN; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME SPECIFICITY; PROTEIN PROTEIN INTERACTION;

EID: 0033038546     PISSN: 03008177     EISSN: None     Source Type: Journal    
DOI: 10.1007/978-1-4419-8624-5_2     Document Type: Article

References (23)

1. Pinna LA: Casein kinase 2: An 'eminence grise' in cellular regulation. Biochim Biophys Acta 1054: 267-284, 1990
2. Tuazon PT, Traugh JA: Casein kinase I and II. Multipotential serine protein kinases: Structure, function, and regulation. In: P. Grengard, G. A. Robinson (eds). Adv Sec Mess Phos Res. Raven Press Ltd, New York, 1991, pp 123-164
3. Issinger O-G: Casein kinases: Pleiotropic mediators of cellular regulation. Pharmalcol Therapeut 59: 1-30, 1993
4. Allende JE, Allende CC: Protein kinase CK2: An enzyme with multiple substrates and a puzzling regulation. FASEB J 9: 313-323, 1995
5. Pinna LA, Meggio F: Protein kinase CK2 ('casein kinase-2') and its implication in cell division and proliferation. In: L. Meijer, S. Guidet, M. Philippe (eds). Progress in Cell Cycle Res. Plenum Press, New York, 1997, pp 1-21
6. Lasa-Benito M, Marin O, Meggio F, Pinna LA: Golgi apparatus mammary gland casein kinase: Monitoring by a specific peptide substrate and definition of specificity determinants: FEBS Lett 382: 149-152, 1996
7. Pinna LA, Ruzzene M: How do protein kinases recognize their substrates? Biochim Biophys Acta 1314: 191-225, 1996
8. Meggio F, Marin O, Pinna LA: Substrate specificity of protein kinase CK2. Cell Mol Biol Res 40: 401-409, 1994
9. Pinna LA, Meggio F, Marchiori F: Type 2 casein kinase: General properties and substrate specificity. In B.E. Kemp (ed). Peptides and protein phosphorylation. CRC press, 1990, pp 145-168
10. Sarno S, Vaglio P, Meggio F, Issinger O-G, Pinna LA: Protein kinase CK2 mutants defective in substrate recognition. Purification and kinetic analysis. J Biol Chem 271: 10595-10601, 1996
11. Sarno S, Vaglio P, Marin O, Issinger O-G, Ruffato K, Pinna LA: Mutational analysis of residues Implicated in the interaction between protein kinase CK2 and peptide substrates. Biochemistry 36: 11717-11724, 1997
12. Vaglio P, Sarno S, Marin O, Meggio F, Issinger O-G, Pinna LA: Mapping the residues of protein kinase CK2 α subunit responsible for responsiveness to polyanionic inhibitors. FEBS Lett 380: 25-28, 1996
13. Sarno S, Vaglio P, Marin O, Meggio F, Issinger O-G, Pinna LA: Basic residues in the 74-83 and 191-198 segments of protein kinase CK2 catalytic subunit are implicated in negative but not in positive regulation by the β-subunit. Eur J Biochem 248: 290-295, 1997
14. Guerra B, Niefind K, Pinna LA, Schomburg D, Issinger O-G: Expression, purification and crystallization of the catalytic subunit of protein kinase CK2 from Z. mays. Acta crystallographica D54: 143-145, 1998
15. Meggio F, Pinna LA: Random tyrosine and glutamic acid containing polymers are very powerful inhibitors of casein kinase-2. Biochim Biophys Acta 1010: 128-130, 1989
16. Miyata Y, Yahara I: interaction between casein kinase II and the 90-kDa stress protein. HSP90. Biochemistry 34: 8123-8129, 1995
17. Li D, Dobrowolska G, Krebs EG: The physical association of casein kinase 2 with nucleolin. J Biol Chem 271: 15662-15668, 1996
18. Knighton DR, Zheng J, Ten Eyck LF, Xuong N-H, Taylor SS, Sowadski JM: Structure of a peptide inhibitor bound to the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase. Science 253: 414-420, 1991
19. Hubbard SR: Crystal structure of the activated insulin receptor tyrosine kinase in complex with peptide substrate and ATP analog. EMBO J 16: 5572-5581, 1997
20. Perich JW, Meggio F, Reynolds EC, 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
21. Gibbs CS, Zoller MJ: Identification of electrostatic interactions that determine the phosphorylation site specificity of cAMP-dependent protein kinase. Biochemistry 30: 5329-5334, 1991
22. Dobrowolska G, Meggio F, Marin O, Lozeman FJ, Li D, Pinna LA, Krebs EG: Substrate recognition by casein kinase II: The role of histidine-160. FEBS Lett 355: 237-241, 1994
23. Niefind K, Guerra B, Pinna LA, Issinger O-G, Schomburg D: Crystal structure of the catalytic subunit of protein kinase CK2 from Zea mays 2.1 Å resolution. EMBO J 17: 2451-2462, 1998