Amino acid conditions near the GPI anchor attachment site of prion protein for the conversion and the GPI anchoring

Biochemical and Biophysical Research Communications

Volumn 391, Issue 4, 2010, Pages 1681-1686

  Hizume, Masaki ^a,b   Kobayashi, Atsushi ^a   Mizusawa, Hidehiro ^b   Kitamoto, Tetsuyuki ^a  

^a TOHOKU UNIVERSITY GRADUATE SCHOOL OF MEDICINE   (Japan)

^b TOKYO MEDICAL AND DENTAL UNIVERSITY   (Japan)

Author keywords

Site; Conversion; Glycosylphosphatidylinositol anchor; Mutation; Prion protein

Indexed keywords

AMINO ACID; GLYCOSYLPHOSPHATIDYLINOSITOL ANCHORED PROTEIN; MUTANT PROTEIN; PRION PROTEIN;

AMINO ACID SUBSTITUTION; ANIMAL CELL; ARTICLE; BINDING SITE; CELL SURFACE; CODON; CONTROLLED STUDY; GENE MUTATION; GENETIC TRANSFECTION; MOUSE; NEUROBLASTOMA CELL; NONHUMAN; PRIORITY JOURNAL; SCRAPIE;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ANIMALS; CRICETINAE; GLYCOSYLPHOSPHATIDYLINOSITOLS; HUMANS; MICE; MICE, MUTANT STRAINS; PRIONS;

CRICETINAE; MURINAE;

EID: 74449092332     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2009.12.128     Document Type: Article

References (26)

1. Prusiner S.B. Prions. Proc. Natl. Acad. Sci. USA 95 (1998) 13363-13383
2. Stahl N., Borchelt D.R., Hsiao K., and Prusiner S.B. Scrapie prion protein contains a phosphatidylinositol glycolipid. Cell 51 (1987) 229-240
3. Orlean P., and Menon A.K. GPI anchoring of protein in yeast and mammalian cells, or: how we learned to stop worrying and love glycophospholipids. J. Lipid Res. 48 (2007) 993-1011
4. Tatzelt J., and Winklhofer K.F. Folding and misfolding of the prion protein in the secretory pathway. Amyloid 11 (2004) 162-172
5. Mead S. Prion disease genetics. Eur. J. Hum. Genet. 14 (2006) 273-281
6. Kitamoto T., Ohta M., Doh-ura K., et al. Novel missense variants of prion protein in Creutzfeldt-Jakob disease or Gerstmann-Sträussler syndrome. Biochem. Biophys. Res. Commun. 191 (1993) 709-714
7. Shiga Y., Satoh K., Kitamoto T., et al. Two different clinical phenotypes of Creutzfeldt-Jakob disease with a M232R substitution. J. Neurol. 254 (2007) 1509-1517
8. Zheng L., Longfei J., Jing Y., et al. PRNP mutations in a series of apparently sporadic neurodegenerative dementias in China. Am. J. Med. Genet. B 147B (2008) 938-944
9. Bratosiewicz J., Liberski P.P., Kulczycki J., and Kordek R. Codon 129 polymorphism of the PRNP gene in normal Polish population and in Creutzfeldt-Jakob disease, and the search for new mutations in PRNP gene. Acta Neurobiol. Exp. (Wars) 61 (2001) 151-156
10. Eisenhaber B., Bork P., and Eisenhaber F. Sequence properties of GPI-anchored proteins near the omega-site: constraints for the polypeptide binding site of the putative transamidase. Protein Eng. 11 (1998) 1155-1161
11. Stahl N., Baldwin M.A., Burlingame A.L., and Prusiner S.B. Identification of glycoinositol phospholipid linked and truncated forms of the scrapie prion protein. Biochemistry 29 (1990) 8879-8884
12. Taylor D.R., and Hooper N.M. The prion protein and lipid rafts. Mol. Membr. Biol. 23 (2006) 89-99
13. Butler D.A., Scott M.R., Bockman J.M., et al. Scrapie-infected murine neuroblastoma cells produce protease-resistant prion proteins. J. Virol. 62 (1988) 1558-1564
14. Ikeda S., Kobayashi A., and Kitamoto T. Thr but Asn of the N-glycosylation sites of PrP is indispensable for its misfolding. Biochem. Biophys. Res. Commun. 369 (2008) 1195-1198
15. Kascsak R.J., Rubenstein R., Merz P.A., et al. Mouse polyclonal and monoclonal antibody to scrapie-associated fibril proteins. J. Virol. 61 (1987) 3688-3693
16. Scott M.R., Köhler R., Foster D., and Prusiner S.B. Chimeric prion protein expression in cultured cells and transgenic mice. Protein Sci. 1 (1992) 986-997
17. Asano M., Mohri S., Ironside J.W., et al. vCJD prion acquires altered virulence through trans-species infection. Biochem. Biophys. Res. Commun. 342 (2006) 293-299
18. Kinoshita T., Fujita M., and Maeda Y. Biosynthesis, remodelling and functions of mammalian GPI-anchored proteins: recent progress. J. Biochem. 144 (2008) 287-294
19. Lowe M.E. Site-specific mutations in the COOH-terminus of placental alkaline phosphatase: a single amino acid change converts a phosphatidylinositol-glycan-anchored protein to a secreted protein. J. Cell Biol. 116 (1992) 799-807
20. Micanovic R., Gerber L.D., Berger J., Kodukula K., and Udenfriend S. Selectivity of the cleavage/attachment site of phosphatidylinositol-glycan-anchored membrane proteins determined by site-specific mutagenesis at Asp-484 of placental alkaline phosphatase. Proc. Natl. Acad. Sci. USA 87 (1990) 157-161
21. Winklhofer K.F., Heske J., Heller U., et al. Determinants of the in vivo folding of the prion protein. A bipartite function of helix 1 in folding and aggregation. J. Biol. Chem. 278 (2003) 14961-14970
22. Chesebro B., Trifilo M., Race R., et al. Anchorless prion protein results in infectious amyloid disease without clinical scrapie. Science 308 (2005) 1435-1439
23. Kiachopoulos S., Bracher A., Winklhofer K.F., and Tatzelt J. Pathogenic mutations located in the hydrophobic core of the prion protein interfere with folding and attachment of the glycosylphosphatidylinositol anchor. J. Biol. Chem. 280 (2005) 9320-9329
24. Field M.C., Moran P., Li W., Keller G.A., and Caras I.W. Retention and degradation of proteins containing an uncleaved glycosylphosphatidylinositol signal. J. Biol. Chem. 269 (1994) 10830-10837
25. Nakatsukasa K., and Brodsky J.L. The recognition and retrotranslocation of misfolded proteins from the endoplasmic reticulum. Traffic 9 (2008) 861-870
26. Kang S.W., Rane N.S., Kim S.J., et al. Substrate-specific translocational attenuation during ER stress defines a pre-emptive quality control pathway. Cell 127 (2006) 999-1013