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Volumn 117, Issue 11, 2004, Pages 2411-2416

Scrapie-like prion protein is translocated to the nuclei of infected cells independently of proteasome inhibition and interacts with chromatin

Author keywords

Microtubules; Nucleus; Prion

Indexed keywords

NUCLEAR PROTEIN; PRION PROTEIN; PROTEASOME; PROTEINASE;

EID: 3042595161     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: 10.1242/jcs.01094     Document Type: Article
Times cited : (76)

References (38)
  • 1
    • 0035897407 scopus 로고    scopus 로고
    • Integrin-mediated adhesion regulates ERK nuclear translocation and phosphorylation of Elk-1
    • Aplin, A. E., Stewart, S. A., Assoian, R. K. and Juliano, R. L. (2001). Integrin-mediated adhesion regulates ERK nuclear translocation and phosphorylation of Elk-1. J. Cell Biol. 153, 273-282.
    • (2001) J. Cell Biol. , vol.153 , pp. 273-282
    • Aplin, A.E.1    Stewart, S.A.2    Assoian, R.K.3    Juliano, R.L.4
  • 3
    • 0037064026 scopus 로고    scopus 로고
    • Stimulation of PrP(C) retrograde transport toward the endoplasmic reticulum increases accumulation of PrP(Sc) in prion-infected cells
    • Beranger, F., Mange, A., Goud, B. and Lehmann, S. (2002). Stimulation of PrP(C) retrograde transport toward the endoplasmic reticulum increases accumulation of PrP(Sc) in prion-infected cells. J. Biol. Chem. 277, 38972-38977.
    • (2002) J. Biol. Chem. , vol.277 , pp. 38972-38977
    • Beranger, F.1    Mange, A.2    Goud, B.3    Lehmann, S.4
  • 4
    • 0028034042 scopus 로고
    • Association of nuclear matrix antigens with exon-containing splicing complexes
    • Blencowe, B. J., Nickerson, J. A., Issner, R., Penman, S. and Sharp, P. A. (1994). Association of nuclear matrix antigens with exon-containing splicing complexes. J. Cell Biol. 127, 593-607.
    • (1994) J. Cell Biol. , vol.127 , pp. 593-607
    • Blencowe, B.J.1    Nickerson, J.A.2    Issner, R.3    Penman, S.4    Sharp, P.A.5
  • 5
    • 0032080434 scopus 로고    scopus 로고
    • Prion protein fragment interacts with PrP-deficient cells
    • Brown, D. R., Schmidt, B. and Kretzschmar, H. A. (1998). Prion protein fragment interacts with PrP-deficient cells. J. Neurosci. Res. 52, 260-267.
    • (1998) J. Neurosci. Res. , vol.52 , pp. 260-267
    • Brown, D.R.1    Schmidt, B.2    Kretzschmar, H.A.3
  • 7
    • 0038699018 scopus 로고    scopus 로고
    • Role of the cytoskeleton in nuclear import
    • Campbell, E. M. and Hope, T. J. (2003). Role of the cytoskeleton in nuclear import. Adv. Drug Deliv. Rev. 55, 761-771.
    • (2003) Adv. Drug Deliv. Rev. , vol.55 , pp. 761-771
    • Campbell, E.M.1    Hope, T.J.2
  • 8
    • 0024545093 scopus 로고
    • Prion protein biosynthesis in scrapie-infected and uninfected neuroblastoma cells
    • Caughey, B., Race, R. E., Ernst, D., Buchmeier, M. J. and Chesebro, B. (1989). Prion protein biosynthesis in scrapie-infected and uninfected neuroblastoma cells. J. Virol. 63, 175-181.
    • (1989) J. Virol. , vol.63 , pp. 175-181
    • Caughey, B.1    Race, R.E.2    Ernst, D.3    Buchmeier, M.J.4    Chesebro, B.5
  • 10
    • 0037415754 scopus 로고    scopus 로고
    • Scrapie-like prion protein accumulates in aggresomes of cyclosporin A- treated cells
    • Cohen, E. and Taraboulos, A. (2003). Scrapie-like prion protein accumulates in aggresomes of cyclosporin A- treated cells. EMBO J. 22, 404-417.
    • (2003) EMBO J. , vol.22 , pp. 404-417
    • Cohen, E.1    Taraboulos, A.2
  • 12
    • 0035966046 scopus 로고    scopus 로고
    • DNA converts cellular prion protein into the beta-sheet conformation and inhibits prion peptide aggregation
    • Cordeiro, Y., Machado, F., Juliano, L., Juliano, M. A., Brentani, R. R., Foguel, D. and Silva, J. L. (2001). DNA converts cellular prion protein into the beta-sheet conformation and inhibits prion peptide aggregation. J. Biol. Chem. 276, 49400-49409.
    • (2001) J. Biol. Chem. , vol.276 , pp. 49400-49409
    • Cordeiro, Y.1    Machado, F.2    Juliano, L.3    Juliano, M.A.4    Brentani, R.R.5    Foguel, D.6    Silva, J.L.7
  • 13
    • 0038159514 scopus 로고    scopus 로고
    • Mutant PrP is delayed in its exit from the endoplasmic reticulum, but neither wild-type nor mutant PrP undergoes retrotranslocation prior to proteasomal degradation
    • Drisaldi, B., Stewart, R. S., Adles, C., Stewart, L. R., Quaglio, E., Biasini, E., Fioriti, L., Chiesa, R. and Harris, D. A. (2003). Mutant PrP is delayed in its exit from the endoplasmic reticulum, but neither wild-type nor mutant PrP undergoes retrotranslocation prior to proteasomal degradation. J. Biol. Chem. 278, 21732-21743.
    • (2003) J. Biol. Chem. , vol.278 , pp. 21732-21743
    • Drisaldi, B.1    Stewart, R.S.2    Adles, C.3    Stewart, L.R.4    Quaglio, E.5    Biasini, E.6    Fioriti, L.7    Chiesa, R.8    Harris, D.A.9
  • 19
    • 0035195010 scopus 로고    scopus 로고
    • Welcome to the nucleus: CAN I take your coat?
    • Harel, A. and Forbes, D. J. (2001). Welcome to the nucleus: CAN I take your coat? Nat. Cell Biol. 3, E267-E269.
    • (2001) Nat. Cell Biol. , vol.3
    • Harel, A.1    Forbes, D.J.2
  • 22
    • 0035800022 scopus 로고    scopus 로고
    • Differential chromatin association and nucleosome binding of the maize HMGA, HMGB, and SSRP1 proteins
    • Lichota, J. and Grasser, K. D. (2001). Differential chromatin association and nucleosome binding of the maize HMGA, HMGB, and SSRP1 proteins. Biochemistry 40, 7860-7867.
    • (2001) Biochemistry , vol.40 , pp. 7860-7867
    • Lichota, J.1    Grasser, K.D.2
  • 23
    • 0037041014 scopus 로고    scopus 로고
    • Cellular phenotyping of secretory and nuclear prion proteins associated with inherited prion diseases
    • Lorenz, H., Windl, O. and Kretzschmar, H. A. (2002). Cellular phenotyping of secretory and nuclear prion proteins associated with inherited prion diseases. J. Biol. Chem. 277, 8508-8516.
    • (2002) J. Biol. Chem. , vol.277 , pp. 8508-8516
    • Lorenz, H.1    Windl, O.2    Kretzschmar, H.A.3
  • 24
    • 0035910069 scopus 로고    scopus 로고
    • Wild-type PrP and a mutant associated with prion disease are subject to retrograde transport and proteasome degradation
    • Ma, J. and Lindquist, S. (2001). Wild-type PrP and a mutant associated with prion disease are subject to retrograde transport and proteasome degradation. Proc. Natl. Acad. Sci. USA 98, 14955-14960.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 14955-14960
    • Ma, J.1    Lindquist, S.2
  • 25
    • 0037195647 scopus 로고    scopus 로고
    • Neurotoxicity and neurodegeneration when PrP accumulates in the cytosol
    • Ma, J., Wollmann, R. and Lindquist, S. (2002). Neurotoxicity and neurodegeneration when PrP accumulates in the cytosol. Science 298, 1781-1785.
    • (2002) Science , vol.298 , pp. 1781-1785
    • Ma, J.1    Wollmann, R.2    Lindquist, S.3
  • 26
    • 0036124813 scopus 로고    scopus 로고
    • Oxidative stress and the prion protein in transmissible spongiform encephalopathies
    • Milhavet, O. and Lehmann, S. (2002). Oxidative stress and the prion protein in transmissible spongiform encephalopathies. Brain Res. Brain Res. Rev. 38, 328-339.
    • (2002) Brain Res. Brain Res. Rev. , vol.38 , pp. 328-339
    • Milhavet, O.1    Lehmann, S.2
  • 28
    • 0033988236 scopus 로고    scopus 로고
    • Successful transmission of three mouse-adapted scrapie strains to murine neuroblastoma cell lines overexpressing wild-type mouse prion protein
    • Nishida, N., Harris, D. A., Vilette, D., Laude, H., Frobert, Y., Grassi, J., Casanova, D., Milhavet, O. and Lehmann, S. (2000). Successful transmission of three mouse-adapted scrapie strains to murine neuroblastoma cell lines overexpressing wild-type mouse prion protein. J. Virol. 74, 320-325.
    • (2000) J. Virol. , vol.74 , pp. 320-325
    • Nishida, N.1    Harris, D.A.2    Vilette, D.3    Laude, H.4    Frobert, Y.5    Grassi, J.6    Casanova, D.7    Milhavet, O.8    Lehmann, S.9
  • 29
    • 0036854702 scopus 로고    scopus 로고
    • The transcriptional activation of the human copper/zinc superoxide dismutase gene by 2,3,7,8-tetrachlorodibenzo-p-dioxin through two different regulator sites, the antioxidant responsive element and xenobiotic responsive element
    • Park, E. Y. and Rho, H. M. (2002). The transcriptional activation of the human copper/zinc superoxide dismutase gene by 2,3,7,8-tetrachlorodibenzo-p-dioxin through two different regulator sites, the antioxidant responsive element and xenobiotic responsive element. Mol. Cell Biochem. 240, 47-55.
    • (2002) Mol. Cell Biochem. , vol.240 , pp. 47-55
    • Park, E.Y.1    Rho, H.M.2
  • 30
    • 0027410936 scopus 로고
    • Kinetics of expression of prion protein in uninfected and scrapie-infected N2a mouse neuroblastoma cells
    • Pfeifer, K., Bachmann, M., Schroder, H. C., Forrest, J. and Muller, W. E. (1993). Kinetics of expression of prion protein in uninfected and scrapie-infected N2a mouse neuroblastoma cells. Cell Biochem. Funct. 11, 1-11.
    • (1993) Cell Biochem. Funct. , vol.11 , pp. 1-11
    • Pfeifer, K.1    Bachmann, M.2    Schroder, H.C.3    Forrest, J.4    Muller, W.E.5
  • 32
    • 0023091197 scopus 로고
    • Characterization of scrapie infection in mouse neuroblastoma cells
    • Race, R. E., Fadness, L. H. and Chesebro, B. (1987). Characterization of scrapie infection in mouse neuroblastoma cells. J. Gen. Virol. 68, 1391-1399.
    • (1987) J. Gen. Virol. , vol.68 , pp. 1391-1399
    • Race, R.E.1    Fadness, L.H.2    Chesebro, B.3
  • 33
    • 0027194968 scopus 로고
    • Nucleic acid binding proteins in highly purified Creutzfeldt-Jakob disease preparations
    • Sklaviadis, T., Akowitz, A., Manuelidis, E. E. and Manuelidis, L. (1993). Nucleic acid binding proteins in highly purified Creutzfeldt-Jakob disease preparations. Proc. Natl. Acad. Sci. USA 90, 5713-5717.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 5713-5717
    • Sklaviadis, T.1    Akowitz, A.2    Manuelidis, E.E.3    Manuelidis, L.4
  • 34
    • 0025373111 scopus 로고
    • Scrapie prion proteins accumulate in the cytoplasm of persistently infected cultured cells
    • Taraboulos, A., Serban, D. and Prusiner, S. B. (1990). Scrapie prion proteins accumulate in the cytoplasm of persistently infected cultured cells. J. Cell Biol. 110, 2117-2132.
    • (1990) J. Cell Biol. , vol.110 , pp. 2117-2132
    • Taraboulos, A.1    Serban, D.2    Prusiner, S.B.3
  • 35
    • 0034090935 scopus 로고    scopus 로고
    • Association of human origin recognition complex 1 with chromatin DNA and nuclease-resistant nuclear structures
    • Tatsumi, Y., Tsurimoto, T., Shirahige, K., Yoshikawa, H. and Obuse, C. (2000). Association of human origin recognition complex 1 with chromatin DNA and nuclease-resistant nuclear structures. J. Biol. Chem. 275, 5904-5910.
    • (2000) J. Biol. Chem. , vol.275 , pp. 5904-5910
    • Tatsumi, Y.1    Tsurimoto, T.2    Shirahige, K.3    Yoshikawa, H.4    Obuse, C.5
  • 36
    • 0035476688 scopus 로고    scopus 로고
    • Proteasomes and ubiquitin are involved in the turnover of the wild-type prion protein
    • Yedidia, Y., Horonchik, L., Tzaban, S., Yanai, A. and Taraboulos, A. (2001). Proteasomes and ubiquitin are involved in the turnover of the wild-type prion protein. EMBO J. 20, 5383-5391.
    • (2001) EMBO J. , vol.20 , pp. 5383-5391
    • Yedidia, Y.1    Horonchik, L.2    Tzaban, S.3    Yanai, A.4    Taraboulos, A.5
  • 38
    • 0033551776 scopus 로고    scopus 로고
    • Proteasomal degradation and N-terminal protease resistance of the codon 145 mutant prion protein
    • Zanusso, G., Petersen, R. B., Jin, T., Jing, Y., Kanoush, R., Ferrari, S., Gambetti, P. and Singh, N. (1999). Proteasomal degradation and N-terminal protease resistance of the codon 145 mutant prion protein. J. Biol. Chem. 274, 23396-23404.
    • (1999) J. Biol. Chem. , vol.274 , pp. 23396-23404
    • Zanusso, G.1    Petersen, R.B.2    Jin, T.3    Jing, Y.4    Kanoush, R.5    Ferrari, S.6    Gambetti, P.7    Singh, N.8


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