Identification of cryptic nuclear localization signals in the prion protein

Neurobiology of Disease

Volumn 12, Issue 2, 2003, Pages 133-149

  Gu, Yaping ^a   Hinnerwisch, Joerg ^a   Fredricks, Rebecca ^a   Kalepu, Sudheera ^a   Mishra, Ravi Shankar ^a   Singh, Neena ^a  

^a CASE WESTERN RESERVE UNIVERSITY   (United States)

Author keywords

GFP; Glycosylation; NLS; Nucleus; Prion protein; Protein transport

Indexed keywords

AMINO ACID; BOVINE SERUM ALBUMIN; PRION PROTEIN;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ARTICLE; CELL MEMBRANE; CELLULAR DISTRIBUTION; CONTROLLED STUDY; ENDOPLASMIC RETICULUM; GENETIC TRANSFECTION; HUMAN; HUMAN CELL; NEUROPATHOLOGY; NUCLEAR LOCALIZATION SIGNAL; PRION DISEASE; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN GLYCOSYLATION; PROTEIN LOCALIZATION; STEADY STATE;

EID: 0037343746     PISSN: 09699961     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-9961(02)00014-1     Document Type: Article

References (35)

1. Adam S.A., Marr R.S., Gerace L. Nuclear protein import in permeabilized mammalian cells requires soluble cytoplasmic factors. J. Cell Biol. 111:1990;807-816.
2. Bazan J.F., Fletterick R.J., McKinley M.P., Prusiner S.B. Predicted secondary structure and membrane topology of the scrapie prion protein. Protein Eng. 2:1987;125-135.
3. Chiesa R., Harris D.A. Prion diseases what is the neurotoxic molecule? Neurobiol Dis. 5:2001;743-763.
4. Collinge J. Prion diseases of humans and animals their causes and molecular basis. Annu. Rev. Neurosci. 24:2001;519-550.
5. Donne D.G., Viles J.H., Groth D., Mehlhorn I., James T.L., Cohen F.E., Prusiner S.B., Wright P.E., Dyson H.J. Structure of the recombinant full-length hamster prion protein PrP (29-231) the N terminus is highly flexible. Proc. Natl. Acad. Sci. USA. 94:1997;13452-13457.
6. Ghetti B., Piccardo P., Frangione B., Bugiani O., Giaccone G., Young K., Prelli F., Farlow M.R., Dlouhy S.R., Tagliavini F. Prion protein amyloidosis. Brain Pathol. 6:1996;127-145.
7. Ghetti B., Piccardo P., Spillantini M.G., Ichimiya Y., Porro M., Perini F., Kitamoto T., Tateishi J., Seiler C., Frangione B., Bugiani O., Giaccone G., Prelli F., Goedert M., Dlouhy S.R., Tagliavini F. Vascular variant of prion protein cerebral amyloidosis with tau-positive neurofibrillary tangles the phenotype of t stop codon 145 mutation in PRNP. Proc. Natl. Acad. Sci. USA. 93:1996;744-748.
8. Gorlich D., Mattaj I.W. Nucleocytoplasmic transport. Science. 271:1996;1513-1518.
9. Gu Y., Fujioka H., Mishra R.S., Li R., Singh N. Prion peptide 106-126 modulates the aggregation of cellular prion protein and induces the synthesis of potentially neurotoxic transmembrane PrP. J. Biol. Chem. 277:2002;2275-2286.
10. Ivanova L., Barmada S., Kummer T., Harris D.A. Mutant prion proteins are partially retained in the endoplasmic reticulum. J. Biol. Chem. 276:2001;42409-42421.
11. Jaegly A., Mouthon F., Peyrin J.-M., Camugli B., Deslys J.-P., Dormont D. Search for nuclear localization signal in the prion protein. Mol. Cell. Neurosci. 11:1998;127-133.
12. Jin T., Gu Y., Zanusso G., Sy M., Kumar A., Cohen M., Gambetti P., Singh N. The chaperone protein BiP binds to a mutant prion protein and mediates its degradation by the proteasome. J. Biol. Chem. 275:2000;38699-38704.
13. Kalderon D., Roberts B.L., Richardson W.D., Smith A.E. A short amino acid sequence able to specify nuclear location. Cell. 39:1984;499-509.
14. Lee K.S., Magalhaes A.C., Zanata S.M., Brentani R.R., Martins V.R., Prado M.A. Internalization of mammalian fluorescent cellular prion protein and N-terminal deletion mutants in living cells. J. Neurochem. 79:2001;79-87.
15. Lehmann S., Harris D.A. A mutant prion protein displays an aberrant membrane association when expressed in cultured cells. J. Biol. Chem. 270:1995;24589-24597.
16. Lehmann S., Harris D.A. Two mutant prion proteins expressed in cultured cells acquire biochemical properties reminiscent of the scrapie isoform. Proc. Natl. Acad. Sci. USA. 93:1996;5610-5614.
17. Lehmann S., Harris D.A. Mutant and infectious prion proteins display common biochemical properties in cultured cells. J. Biol. Chem. 271:1996;1633-1637.
18. Lorenz H., Windl O., Kretzschmar H.A. Cellular phenotyping of secretory and nuclear prion proteins associated with inherited prion diseases. J. Biol. Chem. 277:2002;8508-8516.
19. Sc-like conformation in living cells. Nat. Cell Biol. 1:1999;358-361.
20. Ma J., Lindquist S. Wild-type PrP and a mutant associated with prion disease are subject to retrograde transport and proteasome degradation. Proc. Natl. Acad. Sci. USA. 98:2001;14955-14960.
21. Mishra, R.S., Bose, S., Gu, Y., Li, R., Singh, N. In press. Aggresome formation by mutant prion proteins: the unfolding role of proteasomes in familial prion disorders. J. Alzh. Dis. in press.
22. Nakielny S., Dreyfuss G. Transport of proteins and RNAs in and out of the nucleus. Cell. 99:1999;677-690.
23. Negro A., Ballarin C., Bertoli A., Massimino M.A., Sorgato M.C. The metabolism and imaging in live cells of the bovine prion protein in its native form or carrying single amino acid substitutions. Mol. Cell. Neurosci. 17:2001;521-538.
24. Parchi P., Chen S.G., Brown P., Zou W., Capellari S., Budka H., Hainfellner J., Reyes P.F., Golden G.T., Hauw J.J., Gajdusek D.C., Gambetti P. Different patterns of truncated prion protein fragments correlate with distinct phenotypes in P102L Gerstmann-Straussler-Scheinker disease. Proc. Natl. Acad. Sci. USA. 95:1998;8322-8327.
25. Pfeifer K., Bachmann M., Schroder H.C., Forrest J., Muller W.E. Kinetics of expression of prion protein in uninfected and scrapie-infected N2a mouse neuroblastoma cells. Cell. Biochem. Funct. 11:1993;1-11.
26. Pimplikar S.W., Ikonen E., Simons K. Basolateral protein transport in streptolysin O-permeabilized MDCK cells. J. Cell Biol. 125:1994;1025-1035.
27. Prusiner S.B. Prions. Proc. Natl. Acad. Sci. USA. 95:1998;13363-13383.
28. Riek R., Hornemann S., Wider G., Glockshuber R., Wuthrich K. NMR characterization of the full-length recombinant murine prion protein, mPrP(23-231). FEBS Lett. 413:1997;282-288.
29. Singh N., Zanusso G., Chen S.G., Fujioka H., Richardson S., Gambetti P., Petersen R.B. Prion protein aggregation reverted by low temperature in transfected cells carrying a prion protein gene mutation. J. Biol. Chem. 272:1997;28461-28470.
30. Suzuki T., Park H., Hollingsworth N.M., Sternglanz R., Lennarz W.J. PNG1, a yeast gene encoding a highly conserved peptide N-glycanase. J. Cell Biol. 149:2000;1039-1052.
31. Tagliavini F., Lievens P.M.-J., Tranchant C., Warter J.-M., Mohr M., Giaccone G., Perini F., Rossi G., Salmona M., Piccardo P., Ghetti B., Beavis R.C., Bugiani O., Frangione B., Prelli F. A 7kDa prion protein (PrP) fragment, an integral component of the PrP region required for infectivity, is the major amyloid protein in Gerstmann-Straussler-Scheinker disease A117V. J. Biol. Chem. 276:2001;6009-6015.
32. Tagliavini F., Prelli F., Ghiso J., Bugiani O., Serban D., Prusiner S.B., Farlow M.R., Ghetti B., Frangione B. Amyloid protein of Gerstmann-Straussler-Scheinker disease (Indiana kindred) is an 11 kd fragment of prion protein with an N-terminal glycine at codon 58. EMBO J. 10:1991;513-519.
33. Weissmann C. Molecular genetics of transmissible spongiform encephalopathies. J. Biol. Chem. 274:1999;3-6.
34. Yedidia Y., Horonchik L., Tzaban S., Yanai A., Taraboulos A. Proteasomes and ubiquitin are involved in the turnover of the wild-type prion protein. EMBO J. 20:2001;5383-5391.
35. Zanusso G., Petersen R.B., Jin T., Jing Y., Kanoush R., Ferrari S., Gambetti P., Singh N. Proteasomal degradation and N-terminal protease resistance of the codon 145 mutant prion protein. J. Biol. Chem. 274:1999;23396-23404.