메뉴 건너뛰기




Volumn 19, Issue 2, 1998, Pages 148-154

Chaperone suppression of aggregation and altered subcellular proteasome localization imply protein misfolding in SCA1

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; PROTEASOME;

EID: 0031838352     PISSN: 10614036     EISSN: None     Source Type: Journal    
DOI: 10.1038/502     Document Type: Article
Times cited : (767)

References (44)
  • 1
    • 0031461082 scopus 로고    scopus 로고
    • Biology of A beta amyloid in Alzheimer's disease
    • Wisniewski, T., Ghiso, J. & Frangione, B. Biology of A beta amyloid in Alzheimer's disease. Neurobiol. Dis. 4, 313-328 (1997).
    • (1997) Neurobiol. Dis. , vol.4 , pp. 313-328
    • Wisniewski, T.1    Ghiso, J.2    Frangione, B.3
  • 2
    • 0030744876 scopus 로고    scopus 로고
    • Mutation in the α-synuclein gene identified in families with parkinson's disease
    • Polymeropoulos, M.H. et al. Mutation in the α-Synuclein Gene Identified in Families with Parkinson's Disease. Science 276, 2045-2047 (1997).
    • (1997) Science , vol.276 , pp. 2045-2047
    • Polymeropoulos, M.H.1
  • 3
    • 0030822582 scopus 로고    scopus 로고
    • Prion diseases and the BSE crisis
    • Prusiner, S.B. Prion diseases and the BSE crisis. Science 278, 245-251 (1997).
    • (1997) Science , vol.278 , pp. 245-251
    • Prusiner, S.B.1
  • 4
    • 18544410106 scopus 로고    scopus 로고
    • Formation of neuronal intranuclear inclusions underlies the neurological dysfunction in mice transgenic for the HD mutation
    • Davies, S.W. et al. Formation of neuronal intranuclear inclusions underlies the neurological dysfunction in mice transgenic for the HD mutation. Cell 90, 537-548 (1997).
    • (1997) Cell , vol.90 , pp. 537-548
    • Davies, S.W.1
  • 5
    • 0030752709 scopus 로고    scopus 로고
    • Aggregation of Huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain
    • DiFiglia, M. et al. Aggregation of Huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain. Science 277, 1990-1993 (1997).
    • (1997) Science , vol.277 , pp. 1990-1993
    • DiFiglia, M.1
  • 6
    • 17344362229 scopus 로고    scopus 로고
    • Suppression of aggregate formation and apoptosis by transglutaminase inhibitors in cells expressing truncated DRPLA protein with an expanded polyglutamine stretch
    • Igarashi, S. et al. Suppression of aggregate formation and apoptosis by transglutaminase inhibitors in cells expressing truncated DRPLA protein with an expanded polyglutamine stretch. Nature Genet. 18, 111-117 (1998).
    • (1998) Nature Genet. , vol.18 , pp. 111-117
    • Igarashi, S.1
  • 7
    • 0030666001 scopus 로고    scopus 로고
    • Ataxin-1 with extra glutamines induces alterations in nuclear matrix-associated structures
    • Skinner, P.J. et al. Ataxin-1 with extra glutamines induces alterations in nuclear matrix-associated structures. Nature 389, 971-974 (1997).
    • (1997) Nature , vol.389 , pp. 971-974
    • Skinner, P.J.1
  • 8
    • 0030850412 scopus 로고    scopus 로고
    • Intranuclear inclusions of expanded polyglutamine protein in spinocerebellar ataxia Type 3
    • Paulson, H.L et al. Intranuclear inclusions of expanded polyglutamine protein in spinocerebellar ataxia Type 3. Neuron 19, 333-334 (1997).
    • (1997) Neuron , vol.19 , pp. 333-334
    • Paulson, H.L.1
  • 9
    • 0029245258 scopus 로고
    • Spinocerebellar ataxia type 1
    • Zoghbi, H.Y. & Orr, H.T. Spinocerebellar ataxia type 1. Semin. Cell Biol. 6, 29-35 (1995).
    • (1995) Semin. Cell Biol. , vol.6 , pp. 29-35
    • Zoghbi, H.Y.1    Orr, H.T.2
  • 10
    • 0028283985 scopus 로고
    • Glutamine repeats as polar zippers: Their possible role in inherited neurodegenerative diseases
    • Perutz, M.F., Johnson, T., Suzuki, M. & Finch, J.T. Glutamine repeats as polar zippers: their possible role in inherited neurodegenerative diseases. Proc. Natl. Acad. Sci. USA 91, 5355-5358 (1994).
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 5355-5358
    • Perutz, M.F.1    Johnson, T.2    Suzuki, M.3    Finch, J.T.4
  • 11
    • 0029059477 scopus 로고
    • Incorporation of glutamine repeats makes protein oligomerize: Implications for neurodegenerative diseases
    • Stott, K., Blackburn, J.M., Butler, P.J.G. & Perutz, M. Incorporation of glutamine repeats makes protein oligomerize: Implications for neurodegenerative diseases. Proc. Natl. Acad. Sci. USA 92, 6509-6513 (1995).
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 6509-6513
    • Stott, K.1    Blackburn, J.M.2    Butler, P.J.G.3    Perutz, M.4
  • 12
    • 0026663539 scopus 로고
    • The ubiquitin system for protein degradation
    • Hershko, A. & Ciechanover, A. The ubiquitin system for protein degradation. Annu. Rev. Biochem. 61, 761-807 (1992).
    • (1992) Annu. Rev. Biochem. , vol.61 , pp. 761-807
    • Hershko, A.1    Ciechanover, A.2
  • 13
    • 0030457014 scopus 로고    scopus 로고
    • Ubiquitin-dependent protein degradation
    • Hochstrasser, M. Ubiquitin-dependent protein degradation. Annu. Rev. Genet. 30, 405-439 (1996).
    • (1996) Annu. Rev. Genet. , vol.30 , pp. 405-439
    • Hochstrasser, M.1
  • 14
    • 0031592946 scopus 로고    scopus 로고
    • Structural and functional effects of PA700 and modular protein on proteasomes
    • Adams, G.M. et al. Structural and Functional Effects of PA700 and Modular Protein on Proteasomes. J. Mol. Biol. 273, 646-657 (1997).
    • (1997) J. Mol. Biol. , vol.273 , pp. 646-657
    • Adams, G.M.1
  • 15
    • 0030016595 scopus 로고    scopus 로고
    • Structure and functions of the 20S and 26S proteasomes
    • Coux, O., Tanaka, K. & Goldberg, A.L. Structure and functions of the 20S and 26S proteasomes. Annu. Rev. Biochem. 65, 801-847 (1996).
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 801-847
    • Coux, O.1    Tanaka, K.2    Goldberg, A.L.3
  • 16
    • 0030898710 scopus 로고    scopus 로고
    • Proteasome inhibition leads to a Heat-shock response, induction of endoplasmic reticulum chaperones, and thermotolerance
    • Bush, K.T., Goldberg, A.L. & Nigam, S.K. Proteasome Inhibition Leads to a Heat-shock Response, Induction of Endoplasmic Reticulum Chaperones, and Thermotolerance. J. Biol. Chem. 272, 9086-9092 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 9086-9092
    • Bush, K.T.1    Goldberg, A.L.2    Nigam, S.K.3
  • 17
    • 0029780370 scopus 로고    scopus 로고
    • Evidence that a rapidly turning over protein, normally degraded by proteasomes, regulates hsp72 gene transcription in HepG2 cells
    • Zhou, M., Wu, X. & Ginsberg, H.N. Evidence that a rapidly turning over protein, normally degraded by proteasomes, regulates hsp72 gene transcription in HepG2 cells. J. Biol. Chem. 271, 247-269 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 247-269
    • Zhou, M.1    Wu, X.2    Ginsberg, H.N.3
  • 18
    • 0002858113 scopus 로고    scopus 로고
    • Proteasome inhibitors cause induction of heat shock proteins and trehalose, Which together confer thermotolerance in saccharomyces cerevisiae
    • Lee, D.H. & Goldberg, A.L. Proteasome Inhibitors Cause Induction of Heat Shock Proteins and Trehalose, Which Together Confer Thermotolerance in Saccharomyces cerevisiae. Mol. Cell. Biol. 18, 30-38 (1998).
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 30-38
    • Lee, D.H.1    Goldberg, A.L.2
  • 19
    • 0032489016 scopus 로고    scopus 로고
    • The Hsp70 and Hsp60 chaperone machines
    • Bukau, B. & Horwich, A.L. The Hsp70 and Hsp60 Chaperone Machines. Cell 92, 351-366 (1998).
    • (1998) Cell , vol.92 , pp. 351-366
    • Bukau, B.1    Horwich, A.L.2
  • 20
    • 0032489556 scopus 로고    scopus 로고
    • The conserved carboxyl terminus and zinc Finger-like domain of the Co-chaperone Ydj1 assist Hsp70 in protein folding
    • Lu, Z. & Cyr, D.M. The Conserved Carboxyl Terminus and Zinc Finger-Like Domain of the Co-chaperone Ydj1 Assist Hsp70 in Protein Folding. J. Biol. Chem. 273, 5970-5978 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 5970-5978
    • Lu, Z.1    Cyr, D.M.2
  • 21
    • 0029992278 scopus 로고    scopus 로고
    • Molecular chaperones in cellular protein folding
    • Hartl, F.U. Molecular chaperones in cellular protein folding. Nature 381, 571-580 (1996).
    • (1996) Nature , vol.381 , pp. 571-580
    • Hartl, F.U.1
  • 22
    • 0027184721 scopus 로고
    • Molecular chaperone functions of heat shock proteins
    • Hendricks, J.P. & Hartl, F.-U. Molecular chaperone functions of heat shock proteins. Annu. Rev. Biochem. 62, 349-384 (1993).
    • (1993) Annu. Rev. Biochem. , vol.62 , pp. 349-384
    • Hendricks, J.P.1    Hartl, F.-U.2
  • 23
    • 0026540796 scopus 로고
    • Involvement of chaperonin dnaK in the rapid degradation of a mutant protein in Escherichia coli
    • Sherman, M.Y. & Goldberg, A.L. Involvement of chaperonin dnaK in the rapid degradation of a mutant protein in Escherichia coli. EMBO J. 11, 71-77 (1992).
    • (1992) EMBO J. , vol.11 , pp. 71-77
    • Sherman, M.Y.1    Goldberg, A.L.2
  • 24
    • 0024226522 scopus 로고
    • Escherichia coli heat shock gene mutants are defective in proteolysis
    • Straus, D.B., Walter, W.A. & Gross, C.A. Escherichia coli heat shock gene mutants are defective in proteolysis. Genes Dev. 2, 1851-1858 (1988).
    • (1988) Genes Dev. , vol.2 , pp. 1851-1858
    • Straus, D.B.1    Walter, W.A.2    Gross, C.A.3
  • 26
    • 0001389495 scopus 로고    scopus 로고
    • Involvement of the molecular chaperone Ydj1 in the Ubiquitin-dependent degradation of Short-lived and abnormal proteins in saccharomyces cerevisiae
    • Lee, D.H., Sherman, M.Y. & Goldberg, A.L. Involvement of the Molecular Chaperone Ydj1 in the Ubiquitin-Dependent Degradation of Short-Lived and Abnormal Proteins in Saccharomyces cerevisiae. Mol. Cell. Biol. 16, 4773-4781 (1996).
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 4773-4781
    • Lee, D.H.1    Sherman, M.Y.2    Goldberg, A.L.3
  • 27
    • 0029163222 scopus 로고
    • SCA1 transgenic mice: A model for neurodegeneration caused by an expanded CAG trinucleotide repeat
    • Burright, E.N. et al. SCA1 transgenic mice: a model for neurodegeneration caused by an expanded CAG trinucleotide repeat. Cell 82, 937-948 (1995).
    • (1995) Cell , vol.82 , pp. 937-948
    • Burright, E.N.1
  • 28
    • 0031105569 scopus 로고    scopus 로고
    • Expression of subunits of the 19S complex and of the PA28 activator in rat skeletal muscle
    • Attaix, D. et al. Expression of subunits of the 19S complex and of the PA28 activator in rat skeletal muscle. Mol. Biol. Rep. 24, 95-98 (1997).
    • (1997) Mol. Biol. Rep. , vol.24 , pp. 95-98
    • Attaix, D.1
  • 29
    • 0027216523 scopus 로고
    • Cloning of a unique human homologue of the Escherichia coli DANJ heat shock protein
    • Chellaiah, A., Davis, A. & Mohanakumar, T. Cloning of a unique human homologue of the Escherichia coli DANJ heat shock protein. Biochim. Biophys. Acta 1174, 111-113 (1993).
    • (1993) Biochim. Biophys. Acta , vol.1174 , pp. 111-113
    • Chellaiah, A.1    Davis, A.2    Mohanakumar, T.3
  • 30
    • 0027254681 scopus 로고
    • Human cDNA encoding DnaJ protein homologue
    • Oh, S., Iwahori, A. & Kato, S. Human cDNA encoding DnaJ protein homologue. Biochim. Biophys. Acta 1174, 114-116 (1993).
    • (1993) Biochim. Biophys. Acta , vol.1174 , pp. 114-116
    • Oh, S.1    Iwahori, A.2    Kato, S.3
  • 31
    • 0026739395 scopus 로고
    • Regulation of Hsp70 function by a eukaryotic DnaJ homolog
    • Cyr, D.M., Lu, X. & Douglas, M.G. Regulation of Hsp70 function by a eukaryotic DnaJ homolog. J. Biol. Chem. 267, 20927-20931 (1992).
    • (1992) J. Biol. Chem. , vol.267 , pp. 20927-20931
    • Cyr, D.M.1    Lu, X.2    Douglas, M.G.3
  • 32
    • 0031008364 scopus 로고    scopus 로고
    • A role for HDJ-2/HSDJ in correcting subnuclear trafficking, transactivation, and transrepression defects of a glucocorticoid receptor zinc finger mutant
    • Tang, Y., Ramakrishnan, C., Thomas, J. & DeFranco, D.B. A Role for HDJ-2/HSDJ in Correcting Subnuclear Trafficking, Transactivation, and Transrepression Defects of a Glucocorticoid Receptor Zinc Finger Mutant. Mol. Biol. Cell 8, 795-809 (1997).
    • (1997) Mol. Biol. Cell , vol.8 , pp. 795-809
    • Tang, Y.1    Ramakrishnan, C.2    Thomas, J.3    DeFranco, D.B.4
  • 33
    • 0031441886 scopus 로고    scopus 로고
    • Interactions of the chaperone Hsp104 with yeast Sup35 and mammalian PrP
    • Schirmer, E.C. & Lindquist, S. Interactions of the chaperone Hsp104 with yeast Sup35 and mammalian PrP. Proc. Natl. Acad. Sci. USA 94, 13932-13937 (1997).
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 13932-13937
    • Schirmer, E.C.1    Lindquist, S.2
  • 34
    • 0031443433 scopus 로고    scopus 로고
    • Chaperone-supervised conversion of prion protein to its protease-resistant form
    • DebBurman, S.K., Raymond, G.J., Caughey, B. & Lindquist, S. Chaperone-supervised conversion of prion protein to its protease-resistant form. Proc. Natl. Acad. Sci. USA 94, 13938-13943 (1997).
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 13938-13943
    • DebBurman, S.K.1    Raymond, G.J.2    Caughey, B.3    Lindquist, S.4
  • 35
    • 0032485258 scopus 로고    scopus 로고
    • Chaperoning brain diseases
    • Welch, W.J. & Gambetti, P. Chaperoning Brain Diseases. Nature 392, 23-24 (1998).
    • (1998) Nature , vol.392 , pp. 23-24
    • Welch, W.J.1    Gambetti, P.2
  • 36
    • 0029052468 scopus 로고
    • Role of the chaperone protein Hsp104 in propagation of the yeast Prion-like factor [psi+]
    • Chernoff, Y.O., Lindquist, S.L., Ono, B., Inge-Vechtomov, S.G. & Liebman, S.W. Role of the Chaperone Protein Hsp104 in Propagation of the Yeast Prion-Like Factor [psi+]. Science 268, 880-883 (1995).
    • (1995) Science , vol.268 , pp. 880-883
    • Chernoff, Y.O.1    Lindquist, S.L.2    Ono, B.3    Inge-Vechtomov, S.G.4    Liebman, S.W.5
  • 37
    • 0028353336 scopus 로고
    • DnaJ-like proteins: Molecular chaperones and specific regulators of Hsp70
    • Cyr, D.M., Langer, T. & Douglas, M.G. DnaJ-like proteins: molecular chaperones and specific regulators of Hsp70. Trends Biochem. Sci. 19, 176-181 (1994).
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 176-181
    • Cyr, D.M.1    Langer, T.2    Douglas, M.G.3
  • 39
    • 0025611307 scopus 로고
    • Induction of heat shock (stress) genes in the mammalian brain by hyperthermia and other traumatic events: A current perspective
    • Brown, I.R. Induction of heat shock (stress) genes in the mammalian brain by hyperthermia and other traumatic events: a current perspective. J. Neurosci. Res. 27, 247-255 (1990).
    • (1990) J. Neurosci. Res. , vol.27 , pp. 247-255
    • Brown, I.R.1
  • 40
    • 0028832017 scopus 로고
    • Cooperation of the molecular chaperone Ydj1 with specific Hsp70 homologs to suppress protein aggregation
    • Cyr, D.M. Cooperation of the molecular chaperone Ydj1 with specific Hsp70 homologs to suppress protein aggregation. FEBS Lett. 359, 129-132 (1995).
    • (1995) FEBS Lett. , vol.359 , pp. 129-132
    • Cyr, D.M.1
  • 41
    • 0030448228 scopus 로고    scopus 로고
    • Cooperative action of Hsp70, Hsp90, and DnaJ proteins in protein renaturation
    • Schumacher, R.J. et al. Cooperative action of Hsp70, Hsp90, and DnaJ proteins in protein renaturation. Biochemistry 35, 14889-14898 (1996).
    • (1996) Biochemistry , vol.35 , pp. 14889-14898
    • Schumacher, R.J.1
  • 42
    • 0030716768 scopus 로고    scopus 로고
    • The cerebellar leucine rich acidic nuclear protein interacts with ataxin-1
    • Matilla, T. et al. The cerebellar leucine rich acidic nuclear protein interacts with ataxin-1. Nature 389, 974-978 (1997).
    • (1997) Nature , vol.389 , pp. 974-978
    • Matilla, T.1
  • 43
    • 0029086522 scopus 로고
    • Sodium dodecyl sulfate (SDS) activation of the 20S proteasome in rat liver
    • Shibatani, T. & Ward, W.F. Sodium dodecyl sulfate (SDS) activation of the 20S proteasome in rat liver. Arch. Biochem. Biophys. 321, 160-166 (1995).
    • (1995) Arch. Biochem. Biophys. , vol.321 , pp. 160-166
    • Shibatani, T.1    Ward, W.F.2
  • 44
    • 0029014180 scopus 로고
    • Expression analysis of the ataxin-1 protein in tissues from normal and spinocerebellar ataxia type 1 individuals
    • Servadio, A. et al. Expression analysis of the ataxin-1 protein in tissues from normal and spinocerebellar ataxia type 1 individuals. Nature Genet. 10, 94-98 (1995).
    • (1995) Nature Genet. , vol.10 , pp. 94-98
    • Servadio, A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.