Susceptibility of the prion protein to enzymic phosphorylation

Biochemical and Biophysical Research Communications

Volumn 271, Issue 2, 2000, Pages 337-341

  Negro, Alessandro ^a   Meggio, Flavio ^a   Bertoli, Alessandro ^a   Battistutta, Roberto ^a   Sorgato, M Catia ^a   Pinna, Lorenzo A ^a  

^a UNIVERSITY OF PADOVA   (Italy)

Author keywords

Bovine prion protein; CK2; Prion disease; Protein kinase; PrP phosphorylation

Indexed keywords

CREATINE KINASE MB; PRION PROTEIN; PROTEIN KINASE; PROTEIN KINASE C; PROTEIN TYROSINE KINASE; RECOMBINANT PROTEIN;

ARTICLE; CATTLE; ENZYME PHOSPHORYLATION; PRIORITY JOURNAL; STOICHIOMETRY;

BOS TAURUS; BOVINAE;

EID: 0034630734     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1006/bbrc.2000.2628     Document Type: Article

References (24)

1. Prusiner, S. B. (1982) Novel proteinaceous infectious particles cause scrapie. Science 216, 136-144.
2. Oesch, B., Westaway, D., Waelchli, M., McKinley, M. P., Kent, S. B. H., Aebersold, R., Barry, R. A., Tempst, P., Teplow, D. B., Hood, L. E., Prusiner, S. B., and Weissmann, C. (1985) A cellular gene encodes scrapie PrP 27-30 protein. Cell 40, 735-746.
3. Stahl, N., Borchelt, D. R., Hsiao, K., and Prusiner, S. B. (1987) Scrapie prion protein contains a phosphatidylinositol glycolipid. Cell 51, 229-240.
4. Griffith, J. S. (1967) Self-replication and scrapie. Nature 215, 1043-1044.
5. Prusiner, S. B. (1991) Molecular biology of prion diseases. Science 252, 1515-1522.
6. Stahl, N., Baldwin, M. A., Teplow, D. B., Hood, L., Gibson, B. W., Burlingame, A. L., and Prusiner, S. B. (1993) Structural studies of the scrapie prion protein using mass spectrometry and amino acid sequencing. Biochemistry 32, 1991-2002.
7. Prusiner, S. B. (1998) Prions. Proc. Natl. Acad. Sci. USA 95, 13363-13383.
8. Baldwin, M. A., Cohen, F. E., and Prusiner, S. B. (1995) Prion protein isoforms, a convergence of biological and structural investigations. J. Biol. Chem. 270, 19197-19200.
9. Marks, F. (Ed.) (1996) Protein Phosphorylation. VCH Weinheim, New York, Basel, Cambridge, Tokyo.
10. Fischer, E. H., Pocker, A., and Saari, J. C. (1970) The structure, function and control of glycogen phosphorylase. Essays Biochem. 6, 23-68.
11. Ballou, L. M., and Fischer, E. H. (1986) Phosphoprotein phosphatases. In The Enzymes (Boyer, P. D., and Krebs, E. G., Eds.), Vol. 17, pp. 311-361, Academic Press, New York.
12. Dayani, N., McNaught, R. W., Shenolikar, S., and Smith, R. G. (1990) Receptor interconversion model of hormone action. 2. Requirement of both kinase and phosphatase activities for conferring estrogen binding activity to the estrogen receptor. Biochemistry 29, 2691-2698.
13. Pinna, L. A., and Ruzzene, M. (1996) How do protein kinases recognize their substrates? Biochim. Biophys. Acta 1314, 191-225.
14. Negro, A., DeFilippis, V., Skaper, S. D., James, P., and Sorgato, M. C. (1997) The complete mature bovine prion protein highly expressed in Escherichia coli: Biochemical and structural studies. FEBS Lett. 412, 359-364.
15. Goldmann, W., Hunter, N., Martin, T., Dawson, M., and Hope, J. (1991) Different forms of the bovine PrP gene have five or six copies of a short, G-C-rich element within the protein-coding exon. J. Gen. Virol. 72, 201-204.
16. Meggio, F., Donella Deana, A., and Pinna, L. A. (1981) Endogenous phosphate acceptor proteins for rat liver cytosolic casein kinases. J. Biol. Chem. 256, 11958-11961.
17. Sarno, S., Marin, O., Ghisellini, P., Meggio, F., and Pinna, L. A. (1998) Biochemical evidence that the N-terminal segments of the alpha subunit and the beta subunit play interchangeable roles in the activation of protein kinase CK2. FEBS Lett. 441, 29-33.
18. Riek, R., Wider, G., Billeter, M., Hornemann, S., Glockshuber, R., and Wüthrich, K. (1998) Prion protein NMR structure and familial human spongiform encephalopathies. Proc. Natl. Acad. Sci. USA 95, 11667-11672.
19. Donne, D. G., Viles, J. H., Groth, D., Mehlhorn, I., James, T. L., Cohen, F. E., Prusiner, S. B., Wright, P. E., and Dyson, H. J. (1997) Structure of the recombinant full-length hamster prion protein PrP (29-231): The N terminus is highly flexible. Proc. Natl. Acad. Sci. USA 94, 13452-13457.
20. Guerra, B., and Issinger, O.-G. (1999) Protein kinase CK2 and its role in cellular proliferation, development and pathology. Electrophoresis 20, 391-408.
21. Huang, Z., Prusiner, S. B., and Cohen, F. E. (1996) Scrapie prions: A three-dimensional model of an infectious fragment. Folding Des. 1, 13-19.
22. Jin, J.-K., Choi, J.-K., Lee, H.-G., Kim, Y.-S., Carp, R. I., and Choi, E.-K. (1999) Increased expression of CaM kinase II alpha in the brains of scrapie-infected mice. Neurosci. Lett. 273, 37-40.
23. Woody, R. W. (1995) Circular dichroism. Methods Enzymol. 246, 34-71.
24. Meggio, F., Boldyreff, B., Marin, O., Pinna, L. A., and Issinger, O.-G. (1992) Role of the beta subunit of casein kinase-2 on the stability and specificity of the recombinant reconstituted holoenzyme. Eur. J. Biochem. 204, 293-297.