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Volumn 15, Issue 3, 2008, Pages 359-370

Reduced Translocation of Nascent Prion Protein During ER Stress Contributes to Neurodegeneration

Author keywords

CELLBIO; HUMDISEASE; PROTEINS

Indexed keywords

PRION PROTEIN;

EID: 51449098355     PISSN: 15345807     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.devcel.2008.06.015     Document Type: Article
Times cited : (112)

References (34)
  • 3
    • 33646127577 scopus 로고    scopus 로고
    • Molecular chaperones and protein quality control
    • Bukau B., Weissman J., and Horwich A. Molecular chaperones and protein quality control. Cell 125 (2006) 443-451
    • (2006) Cell , vol.125 , pp. 443-451
    • Bukau, B.1    Weissman, J.2    Horwich, A.3
  • 4
    • 36049020231 scopus 로고    scopus 로고
    • A general model of prion strains and their pathogenicity
    • Collinge J., and Clarke A.R. A general model of prion strains and their pathogenicity. Science 318 (2007) 930-936
    • (2007) Science , vol.318 , pp. 930-936
    • Collinge, J.1    Clarke, A.R.2
  • 5
    • 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. 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 (2003) 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
  • 6
    • 15744395826 scopus 로고    scopus 로고
    • Cytosolic prion protein (PrP) is not toxic in N2a cells and primary neurons expressing pathogenic PrP mutations
    • Fioriti L., Dossena S., Stewart L.R., Stewart R.S., Harris D.A., Forloni G., and Chiesa R. Cytosolic prion protein (PrP) is not toxic in N2a cells and primary neurons expressing pathogenic PrP mutations. J. Biol. Chem. 280 (2005) 11320-11328
    • (2005) J. Biol. Chem. , vol.280 , pp. 11320-11328
    • Fioriti, L.1    Dossena, S.2    Stewart, L.R.3    Stewart, R.S.4    Harris, D.A.5    Forloni, G.6    Chiesa, R.7
  • 7
    • 0037450802 scopus 로고    scopus 로고
    • Substrate-specific function of the translocon-associated protein complex during translocation across the ER membrane
    • Fons R.D., Bogert B.A., and Hegde R.S. Substrate-specific function of the translocon-associated protein complex during translocation across the ER membrane. J. Cell Biol. 160 (2003) 529-539
    • (2003) J. Cell Biol. , vol.160 , pp. 529-539
    • Fons, R.D.1    Bogert, B.A.2    Hegde, R.S.3
  • 9
    • 0033576323 scopus 로고    scopus 로고
    • Transmissible and genetic prion diseases share a common pathway of neurodegeneration
    • Hegde R.S., Tremblay P., Groth D., DeArmond S.J., Prusiner S.B., and Lingappa V.R. Transmissible and genetic prion diseases share a common pathway of neurodegeneration. Nature 402 (1999) 822-826
    • (1999) Nature , vol.402 , pp. 822-826
    • Hegde, R.S.1    Tremblay, P.2    Groth, D.3    DeArmond, S.J.4    Prusiner, S.B.5    Lingappa, V.R.6
  • 10
    • 33646175291 scopus 로고    scopus 로고
    • Stressing out the ER: a role of the unfolded protein response in prion-related disorders
    • Hetz C.A., and Soto C. Stressing out the ER: a role of the unfolded protein response in prion-related disorders. Curr. Mol. Med. 6 (2006) 37-43
    • (2006) Curr. Mol. Med. , vol.6 , pp. 37-43
    • Hetz, C.A.1    Soto, C.2
  • 11
    • 0142105406 scopus 로고    scopus 로고
    • Caspase-12 and endoplasmic reticulum stress mediate neurotoxicity of pathological prion protein
    • Hetz C., Russelakis-Carneiro M., Maundrell K., Castilla J., and Soto C. Caspase-12 and endoplasmic reticulum stress mediate neurotoxicity of pathological prion protein. EMBO J. 22 (2003) 5435-5445
    • (2003) EMBO J. , vol.22 , pp. 5435-5445
    • Hetz, C.1    Russelakis-Carneiro, M.2    Maundrell, K.3    Castilla, J.4    Soto, C.5
  • 13
    • 33751333201 scopus 로고    scopus 로고
    • Substrate-specific translocational attenuation during ER stress defines a pre-emptive quality control pathway
    • Kang S.W., Rane N.S., Kim S.J., Garrison J.L., Taunton J., and Hegde R.S. Substrate-specific translocational attenuation during ER stress defines a pre-emptive quality control pathway. Cell 127 (2006) 999-1013
    • (2006) Cell , vol.127 , pp. 999-1013
    • Kang, S.W.1    Rane, N.S.2    Kim, S.J.3    Garrison, J.L.4    Taunton, J.5    Hegde, R.S.6
  • 14
    • 0036854303 scopus 로고    scopus 로고
    • Cotranslational partitioning of nascent prion protein into multiple populations at the translocation channel
    • Kim S.J., and Hegde R.S. Cotranslational partitioning of nascent prion protein into multiple populations at the translocation channel. Mol. Biol. Cell 13 (2002) 3775-3786
    • (2002) Mol. Biol. Cell , vol.13 , pp. 3775-3786
    • Kim, S.J.1    Hegde, R.S.2
  • 15
    • 0035854696 scopus 로고    scopus 로고
    • Combinatorial control of prion protein biogenesis by the signal sequence and transmembrane domain
    • Kim S.J., Rahbar R., and Hegde R.S. Combinatorial control of prion protein biogenesis by the signal sequence and transmembrane domain. J. Biol. Chem. 276 (2001) 26132-26140
    • (2001) J. Biol. Chem. , vol.276 , pp. 26132-26140
    • Kim, S.J.1    Rahbar, R.2    Hegde, R.S.3
  • 16
    • 0036481454 scopus 로고    scopus 로고
    • Signal sequences control gating of the protein translocation channel in a substrate-specific manner
    • Kim S.J., Mitra D., Salerno J.R., and Hegde R.S. Signal sequences control gating of the protein translocation channel in a substrate-specific manner. Dev. Cell 2 (2002) 207-217
    • (2002) Dev. Cell , vol.2 , pp. 207-217
    • Kim, S.J.1    Mitra, D.2    Salerno, J.R.3    Hegde, R.S.4
  • 18
    • 11144255136 scopus 로고    scopus 로고
    • The efficiency of protein compartmentalization into the secretory pathway
    • Levine C.G., Mitra D., Sharma A., Smith C.L., and Hegde R.S. The efficiency of protein compartmentalization into the secretory pathway. Mol. Biol. Cell 16 (2005) 279-291
    • (2005) Mol. Biol. Cell , vol.16 , pp. 279-291
    • Levine, C.G.1    Mitra, D.2    Sharma, A.3    Smith, C.L.4    Hegde, R.S.5
  • 20
    • 0032432056 scopus 로고    scopus 로고
    • Ribosome association contributes to restricting mRNAs to the cell body of hippocampal neurons
    • Lu Z., McLaren R.S., Winters C.A., and Ralston E. Ribosome association contributes to restricting mRNAs to the cell body of hippocampal neurons. Mol. Cell. Neurosci. 12 (1998) 363-375
    • (1998) Mol. Cell. Neurosci. , vol.12 , pp. 363-375
    • Lu, Z.1    McLaren, R.S.2    Winters, C.A.3    Ralston, E.4
  • 21
    • 0037195647 scopus 로고    scopus 로고
    • Neurotoxicity and neurodegeneration when PrP accumulates in the cytosol
    • Ma J., Wollmann R., and Lindquist S. Neurotoxicity and neurodegeneration when PrP accumulates in the cytosol. Science 298 (2002) 1781-1785
    • (2002) Science , vol.298 , pp. 1781-1785
    • Ma, J.1    Wollmann, R.2    Lindquist, S.3
  • 22
    • 0242363656 scopus 로고    scopus 로고
    • Depleting neuronal PrP in prion infection prevents disease and reverses spongiosis
    • Mallucci G., Dickinson A., Linehan J., Klohn P.C., Brandner S., and Collinge J. Depleting neuronal PrP in prion infection prevents disease and reverses spongiosis. Science 302 (2003) 871-874
    • (2003) Science , vol.302 , pp. 871-874
    • Mallucci, G.1    Dickinson, A.2    Linehan, J.3    Klohn, P.C.4    Brandner, S.5    Collinge, J.6
  • 25
    • 33750087269 scopus 로고    scopus 로고
    • Conditions of endoplasmic reticulum stress favor the accumulation of cytosolic prion protein
    • Orsi A., Fioriti L., Chiesa R., and Sitia R. Conditions of endoplasmic reticulum stress favor the accumulation of cytosolic prion protein. J. Biol. Chem. 281 (2006) 30431-30438
    • (2006) J. Biol. Chem. , vol.281 , pp. 30431-30438
    • Orsi, A.1    Fioriti, L.2    Chiesa, R.3    Sitia, R.4
  • 27
    • 10644267669 scopus 로고    scopus 로고
    • Protection from cytosolic prion protein toxicity by modulation of protein translocation
    • Rane N.S., Yonkovich J.L., and Hegde R.S. Protection from cytosolic prion protein toxicity by modulation of protein translocation. EMBO J. 23 (2004) 4550-4559
    • (2004) EMBO J. , vol.23 , pp. 4550-4559
    • Rane, N.S.1    Yonkovich, J.L.2    Hegde, R.S.3
  • 28
    • 34250899722 scopus 로고    scopus 로고
    • Signal integration in the endoplasmic reticulum unfolded protein response
    • Ron D., and Walter P. Signal integration in the endoplasmic reticulum unfolded protein response. Nat. Rev. Mol. Cell Biol. 8 (2007) 519-529
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 519-529
    • Ron, D.1    Walter, P.2
  • 29
    • 0142135128 scopus 로고    scopus 로고
    • Cytosolic prion protein is not toxic and protects against Bax-mediated cell death in human primary neurons
    • Roucou X., Guo Q., Zhang Y., Goodyer C.G., and LeBlanc A.C. Cytosolic prion protein is not toxic and protects against Bax-mediated cell death in human primary neurons. J. Biol. Chem. 278 (2003) 40877-40881
    • (2003) J. Biol. Chem. , vol.278 , pp. 40877-40881
    • Roucou, X.1    Guo, Q.2    Zhang, Y.3    Goodyer, C.G.4    LeBlanc, A.C.5
  • 30
    • 0027086835 scopus 로고
    • Chimeric prion protein expression in cultured cells and transgenic mice
    • Scott M.R., Kohler R., Foster D., and Prusiner S.B. Chimeric prion protein expression in cultured cells and transgenic mice. Protein Sci. 1 (1992) 986-997
    • (1992) Protein Sci. , vol.1 , pp. 986-997
    • Scott, M.R.1    Kohler, R.2    Foster, D.3    Prusiner, S.B.4
  • 31
    • 0242412541 scopus 로고    scopus 로고
    • Mutational analysis of topological determinants in prion protein (PrP) and measurement of transmembrane and cytosolic PrP during prion infection
    • Stewart R.S., and Harris D.A. Mutational analysis of topological determinants in prion protein (PrP) and measurement of transmembrane and cytosolic PrP during prion infection. J. Biol. Chem. 278 (2003) 45960-45968
    • (2003) J. Biol. Chem. , vol.278 , pp. 45960-45968
    • Stewart, R.S.1    Harris, D.A.2
  • 32
    • 0034388026 scopus 로고    scopus 로고
    • LHS1 and SIL1 provide a lumenal function that is essential for protein translocation into the endoplasmic reticulum
    • Tyson J.R., and Stirling C.J. LHS1 and SIL1 provide a lumenal function that is essential for protein translocation into the endoplasmic reticulum. EMBO J. 19 (2000) 6440-6452
    • (2000) EMBO J. , vol.19 , pp. 6440-6452
    • Tyson, J.R.1    Stirling, C.J.2
  • 33
    • 0029951178 scopus 로고    scopus 로고
    • Signal sequence-dependent function of the TRAM protein during early phases of protein transport across the endoplasmic reticulum membrane
    • Voigt S., Jungnickel B., Hartmann E., and Rapoport T.A. Signal sequence-dependent function of the TRAM protein during early phases of protein transport across the endoplasmic reticulum membrane. J. Cell Biol. 134 (1996) 25-35
    • (1996) J. Cell Biol. , vol.134 , pp. 25-35
    • Voigt, S.1    Jungnickel, B.2    Hartmann, E.3    Rapoport, T.A.4
  • 34
    • 25144520251 scopus 로고    scopus 로고
    • Protein accumulation and neurodegeneration in the woozy mutant mouse is caused by disruption of SIL1, a cochaperone of BiP
    • Zhao L., Longo-Guess C., Harris B.S., Lee J.W., and Ackerman S.L. Protein accumulation and neurodegeneration in the woozy mutant mouse is caused by disruption of SIL1, a cochaperone of BiP. Nat. Genet. 37 (2005) 974-979
    • (2005) Nat. Genet. , vol.37 , pp. 974-979
    • Zhao, L.1    Longo-Guess, C.2    Harris, B.S.3    Lee, J.W.4    Ackerman, S.L.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.