메뉴 건너뛰기




Volumn 11, Issue 22, 2002, Pages 2689-2700

Aggregate formation inhibits proteasomal degradation of polyglutamine proteins

Author keywords

[No Author keywords available]

Indexed keywords

MUTANT PROTEIN; POLYGLUTAMINE; PROTEASOME; UBIQUITIN;

EID: 0037108725     PISSN: 09646906     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (241)

References (45)
  • 1
    • 0034094873 scopus 로고    scopus 로고
    • Glutamine repeats and neurodegeneration
    • Zoghbi, H.Y. and Orr, H.T. (2000) Glutamine repeats and neurodegeneration. Annu. Rev. Neurosci., 23, 217-247.
    • (2000) Annu. Rev. Neurosci , vol.23 , pp. 217-247
    • Zoghbi, H.Y.1    Orr, H.T.2
  • 2
    • 0033862578 scopus 로고    scopus 로고
    • Insights from mouse models into the molecular basis of neurodegeneration
    • Heintz, N. and Zoghbi, H.Y. (2000) Insights from mouse models into the molecular basis of neurodegeneration. Annu. Rev. Physiol., 62, 779-802.
    • (2000) Annu. Rev. Physiol , vol.62 , pp. 779-802
    • Heintz, N.1    Zoghbi, H.Y.2
  • 3
    • 0036533795 scopus 로고    scopus 로고
    • Lessons from animal models of Huntington's disease
    • Rubinsztein, D.C. (2002) Lessons from animal models of Huntington's disease. Trends Genet, 18, 202-209.
    • (2002) Trends Genet , vol.18 , pp. 202-209
    • Rubinsztein, D.C.1
  • 4
    • 0035139109 scopus 로고    scopus 로고
    • Cellular defenses against unfolded proteins: A cell biologist thinks about neurodegenerative diseases
    • Sherman, M.Y. and Goldberg, A.L. (2001) Cellular defenses against unfolded proteins: a cell biologist thinks about neurodegenerative diseases. Neuron, 29, 15-32.
    • (2001) Neuron , vol.29 , pp. 15-32
    • Sherman, M.Y.1    Goldberg, A.L.2
  • 5
    • 0028283985 scopus 로고
    • Glutamine repeats as polar zippers: Their possible role in inherited neurodegenerative diseases
    • Perutz, M.F., Johnson, T., Suzuki, M. and Finch, J.T. (1994) Glutamine repeats as polar zippers: their possible role in inherited neurodegenerative diseases. Proc. Natl. Acad. Sci. USA, 91, 5355-5358.
    • (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
  • 6
    • 0035833997 scopus 로고    scopus 로고
    • An expanded glutamine repeat destabilizes native ataxin-3 structure and mediates formation of parallel β-fibrils
    • Bevivino, A.E. and Loll, P.J. (2001) An expanded glutamine repeat destabilizes native ataxin-3 structure and mediates formation of parallel β-fibrils. Proc. Natl. Acad. Sci. USA, 98, 11955-11960.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 11955-11960
    • Bevivino, A.E.1    Loll, P.J.2
  • 7
    • 0031838352 scopus 로고    scopus 로고
    • Chaperone suppression of aggregation and altered subcellular proteasome localization imply protein misfolding in SCA1
    • Cummings, C.J., Mancini, M.A., Antalffy, B., DeFranco, D.B., Orr, H.T. and Zoghbi, H.Y. (1998) Chaperone suppression of aggregation and altered subcellular proteasome localization imply protein misfolding in SCA1. Nat. Genet., 19, 148-154.
    • (1998) Nat. Genet , vol.19 , pp. 148-154
    • Cummings, C.J.1    Mancini, M.A.2    Antalffy, B.3    DeFranco, D.B.4    Orr, H.T.5    Zoghbi, H.Y.6
  • 8
  • 9
    • 0032867676 scopus 로고    scopus 로고
    • The 26S proteasome: A molecular machine designed for controlled proteolysis
    • Voges, D., Zwickl, P. and Baumeister, W. (1999) The 26S proteasome: a molecular machine designed for controlled proteolysis. Annu. Rev. Biochem., 68, 1015-1068.
    • (1999) Annu. Rev. Biochem , vol.68 , pp. 1015-1068
    • Voges, D.1    Zwickl, P.2    Baumeister, W.3
  • 10
    • 0035783169 scopus 로고    scopus 로고
    • Mechanisms of disaggregation and refolding of stable protein aggregates by molecular chaperones
    • Ben-Zvi, A.P. and Goloubinoff, P. (2001) Mechanisms of disaggregation and refolding of stable protein aggregates by molecular chaperones. J. Struct. Biol., 135, 84-93.
    • (2001) J. Struct. Biol , vol.135 , pp. 84-93
    • Ben-Zvi, A.P.1    Goloubinoff, P.2
  • 11
    • 0032475931 scopus 로고    scopus 로고
    • Huntingtin acts in the nucleus to induce apoptosis but death does not correlate with the formation of intranuclear inclusions
    • Saudou, F., Finkbeiner, S., Devys, D. and Greenberg, M.E. (1998) Huntingtin acts in the nucleus to induce apoptosis but death does not correlate with the formation of intranuclear inclusions. Cell, 95, 55-66.
    • (1998) Cell , vol.95 , pp. 55-66
    • Saudou, F.1    Finkbeiner, S.2    Devys, D.3    Greenberg, M.E.4
  • 12
    • 0032475877 scopus 로고    scopus 로고
    • Nuclear inclusions in glutamine repeat disorders: Are they pernicious, coincidental, or beneficial?
    • Sisodia, S.S. (1998) Nuclear inclusions in glutamine repeat disorders: are they pernicious, coincidental, or beneficial? Cell, 95, 1-4.
    • (1998) Cell , vol.95 , pp. 1-4
    • Sisodia, S.S.1
  • 13
    • 0033396283 scopus 로고    scopus 로고
    • Intranuclear inclusions and the ubiquitin-proteasome pathway: Digestion of a red herring?
    • Floyd, J.A. and Hamilton, B.A. (1999) Intranuclear inclusions and the ubiquitin-proteasome pathway: digestion of a red herring? Neuron, 24, 765-766.
    • (1999) Neuron , vol.24 , pp. 765-766
    • Floyd, J.A.1    Hamilton, B.A.2
  • 15
    • 0035849879 scopus 로고    scopus 로고
    • Cause of neural death in neurodegenerative diseases attributable to expansion of glutamine repeats
    • Perutz, M.F. and Windle, A.H. (2001) Cause of neural death in neurodegenerative diseases attributable to expansion of glutamine repeats. Nature, 412, 143-144.
    • (2001) Nature , vol.412 , pp. 143-144
    • Perutz, M.F.1    Windle, A.H.2
  • 17
    • 0035947372 scopus 로고    scopus 로고
    • Impairment of the ubiquitin-proteasome system by protein aggregation
    • Bence, N.F., Sampat, R.M. and Kopito, R.R. (2001) Impairment of the ubiquitin-proteasome system by protein aggregation. Science, 292, 1552-1555.
    • (2001) Science , vol.292 , pp. 1552-1555
    • Bence, N.F.1    Sampat, R.M.2    Kopito, R.R.3
  • 18
    • 0035336658 scopus 로고    scopus 로고
    • Altered proteasomal function due to the expression of polyglutamine-expanded truncated N-terminal huntingtin induces apoptosis by caspase activation through mitochondrial cytochrome c release
    • Jana, N.R., Zemskov, E.A., Wang, G. and Nukina, N. (2001) Altered proteasomal function due to the expression of polyglutamine-expanded truncated N-terminal huntingtin induces apoptosis by caspase activation through mitochondrial cytochrome c release. Hum. Mol. Genet., 10, 1049-1059.
    • (2001) Hum. Mol. Genet , vol.10 , pp. 1049-1059
    • Jana, N.R.1    Zemskov, E.A.2    Wang, G.3    Nukina, N.4
  • 19
    • 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
  • 20
    • 0034754875 scopus 로고    scopus 로고
    • Accumulation of mutant huntingtin fragments in aggresome-like inclusion bodies as a result of insufficient protein degradation
    • Waelter, S., Boeddrich, A., Lurz, R., Scherzinger, E., Lueder, G., Lehrach, H. and Wanker, E.E. (2001) Accumulation of mutant huntingtin fragments in aggresome-like inclusion bodies as a result of insufficient protein degradation. Mol. Biol. Cell, 12, 1393-1407.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 1393-1407
    • Waelter, S.1    Boeddrich, A.2    Lurz, R.3    Scherzinger, E.4    Lueder, G.5    Lehrach, H.6    Wanker, E.E.7
  • 21
    • 0035818579 scopus 로고    scopus 로고
    • Specificity in intracellular protein aggregation and inclusion body formation
    • Rajan, R.S., Illing, M.E., Bence, N.F. and Kopito, R.R. (2001) Specificity in intracellular protein aggregation and inclusion body formation. Proc. Natl. Acad. Sci. USA, 98, 13060-13065.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 13060-13065
    • Rajan, R.S.1    Illing, M.E.2    Bence, N.F.3    Kopito, R.R.4
  • 22
    • 0344466781 scopus 로고    scopus 로고
    • Characterization and dynamics of aggresome formation by a cytosolic GFP-chimera
    • Garcia-Mata, R., Bebok, Z., Sorscher, E.J. and Sztul, E.S. (1999) Characterization and dynamics of aggresome formation by a cytosolic GFP-chimera. J. Cell Biol., 146, 1239-1254.
    • (1999) J. Cell Biol , vol.146 , pp. 1239-1254
    • Garcia-Mata, R.1    Bebok, Z.2    Sorscher, E.J.3    Sztul, E.S.4
  • 23
    • 0032576605 scopus 로고    scopus 로고
    • Aggresomes: A cellular response to misfolded. proteins
    • Johnston, J.A., Ward, C.L. and Kopito, R.R. (1998) Aggresomes: a cellular response to misfolded. proteins. J. Cell Biol., 143, 1883-1898.
    • (1998) J. Cell Biol , vol.143 , pp. 1883-1898
    • Johnston, J.A.1    Ward, C.L.2    Kopito, R.R.3
  • 24
    • 0030775380 scopus 로고    scopus 로고
    • Inhibition of ubiquitin/proteasome-dependent protein degradation by the Gly-Ala repeat domain of the Epstein-Barr virus nuclear antigen 1
    • Levitskaya, J., Sharipo, A., Leonchiks, A., Ciechanover, A. and Masucci, M.G. (1997) Inhibition of ubiquitin/proteasome-dependent protein degradation by the Gly-Ala repeat domain of the Epstein-Barr virus nuclear antigen 1. Proc. Natl. Acad. Sci. USA, 94, 12616-12621.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 12616-12621
    • Levitskaya, J.1    Sharipo, A.2    Leonchiks, A.3    Ciechanover, A.4    Masucci, M.G.5
  • 25
    • 0031904016 scopus 로고    scopus 로고
    • A minimal glycine-alanine repeat prevents the interaction of ubiquitinated 1κB-α with the proteasome: A new mechanism for selective inhibition of proteolysis
    • Sharipo, A., Imreh, M., Leonchiks, A., Imreh, S. and Masucci, M.G. (1998) A minimal glycine-alanine repeat prevents the interaction of ubiquitinated 1κB-α with the proteasome: a new mechanism for selective inhibition of proteolysis. Nat. Med., 4, 939-944.
    • (1998) Nat. Med , vol.4 , pp. 939-944
    • Sharipo, A.1    Imreh, M.2    Leonchiks, A.3    Imreh, S.4    Masucci, M.G.5
  • 26
    • 0033391428 scopus 로고    scopus 로고
    • Mutation of the E6-AP ubiquitin ligase reduces nuclear inclusion frequency while accelerating polyglutamine-induced pathology in SCA1 mice
    • Cummings, C.J., Reinstein, E., Sun, Y., Antalffy, B., Jiang, Y., Ciehanover, A., Orr, H.T., Beaudet, A.L. and Zoghbi, H.Y. (1999) Mutation of the E6-AP ubiquitin ligase reduces nuclear inclusion frequency while accelerating polyglutamine-induced pathology in SCA1 mice. Neuron, 24, 879-892.
    • (1999) Neuron , vol.24 , pp. 879-892
    • Cummings, C.J.1    Reinstein, E.2    Sun, Y.3    Antalffy, B.4    Jiang, Y.5    Ciehanover, A.6    Orr, H.T.7    Beaudet, A.L.8    Zoghbi, H.Y.9
  • 27
    • 0034023407 scopus 로고    scopus 로고
    • Short-lived green fluorescent proteins for quantification of ubiquitin/proteasome-dependent proteolysis in living cells
    • Dantuma, N.P., Lindsten, K., Glas, R., Jellne, M. and Masucci, M.G. (2000) Short-lived green fluorescent proteins for quantification of ubiquitin/proteasome-dependent proteolysis in living cells. Nat. Biotechnol., 18, 538-543.
    • (2000) Nat. Biotechnol , vol.18 , pp. 538-543
    • Dantuma, N.P.1    Lindsten, K.2    Glas, R.3    Jellne, M.4    Masucci, M.G.5
  • 28
    • 0029861143 scopus 로고    scopus 로고
    • The N-end rule: Functions, mysteries, uses
    • Varshavsky, A. (1996) The N-end rule: functions, mysteries, uses. Proc. Natl. Acad. Sci. USA, 93, 12142-12149.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 12142-12149
    • Varshavsky, A.1
  • 29
    • 0034682502 scopus 로고    scopus 로고
    • Inhibition of proteasomal degradation by the Gly-Ala repeat of Epstein-Baff virus is influenced by the length of the repeat and the strength of the degradation signal
    • Dantuma, N.P., Heessen, S., Lindsten, K., Jellne, M. and Masucci, M.G. (2000) Inhibition of proteasomal degradation by the Gly-Ala repeat of Epstein-Baff virus is influenced by the length of the repeat and the strength of the degradation signal. Proc. Natl. Acad. Sci. USA, 97, 8381-8385.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 8381-8385
    • Dantuma, N.P.1    Heessen, S.2    Lindsten, K.3    Jellne, M.4    Masucci, M.G.5
  • 30
    • 0031010398 scopus 로고    scopus 로고
    • Covalent modification of the active site threonine of proteasomal β subunits and the Escherichia coli homolog Hs1V by a new class of inhibitors
    • Bogyo, M., McMaster, J.S., Gaczynska, M., Tortorella, D., Goldberg, A.L. and Ploegh, H. (1997) Covalent modification of the active site threonine of proteasomal β subunits and the Escherichia coli homolog Hs1V by a new class of inhibitors. Proc. Natl. Acad. Sci. USA, 94, 6629-6634.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 6629-6634
    • Bogyo, M.1    McMaster, J.S.2    Gaczynska, M.3    Tortorella, D.4    Goldberg, A.L.5    Ploegh, H.6
  • 33
    • 0030841343 scopus 로고    scopus 로고
    • Conformational disease
    • Carrell, R.W. and Lomas, D.A. (1997) Conformational disease. Lancet, 350, 134-138.
    • (1997) Lancet , vol.350 , pp. 134-138
    • Carrell, R.W.1    Lomas, D.A.2
  • 35
    • 0036501074 scopus 로고    scopus 로고
    • Molecular chaperones enhance the degradation of expanded polyglutamine repeat androgen receptor in a cellular model of spinal and bulbar muscular atrophy
    • Bailey, C.K., Andriola, I.F., Kampinga, H.H. and Merry, D.E. (2002) Molecular chaperones enhance the degradation of expanded polyglutamine repeat androgen receptor in a cellular model of spinal and bulbar muscular atrophy. Hum. Mol. Genet., 11, 515-523.
    • (2002) Hum. Mol. Genet , vol.11 , pp. 515-523
    • Bailey, C.K.1    Andriola, I.F.2    Kampinga, H.H.3    Merry, D.E.4
  • 36
    • 0030908095 scopus 로고    scopus 로고
    • Models of amyloid seeding in Alzheimer's disease and scrapie: Mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins
    • Harper, J.D. and Lansbury, P.T., Jr (1997) Models of amyloid seeding in Alzheimer's disease and scrapie: mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins. Annu. Rev. Biochem., 66, 385-407.
    • (1997) Annu. Rev. Biochem , vol.66 , pp. 385-407
    • Harper, J.D.1    Lansbury P.T., Jr.2
  • 37
    • 0035266072 scopus 로고    scopus 로고
    • ATP-dependent proteases degrade their substrates by processively unraveling them from the degradation signal
    • Lee, C., Schwartz, M.P., Prakash, S., Iwakura, M. and Matouschek, A. (2001) ATP-dependent proteases degrade their substrates by processively unraveling them from the degradation signal. Mol. Cell, 7, 627-637.
    • (2001) Mol. Cell , vol.7 , pp. 627-637
    • Lee, C.1    Schwartz, M.P.2    Prakash, S.3    Iwakura, M.4    Matouschek, A.5
  • 38
    • 0035694696 scopus 로고    scopus 로고
    • Proteins are unfolded on the surface of the ATPase ring before transport into the proteasome
    • Navon, A. and Goldberg, A.L. (2001) Proteins are unfolded on the surface of the ATPase ring before transport into the proteasome. Mol. Cell, 8, 1339-1349.
    • (2001) Mol. Cell , vol.8 , pp. 1339-1349
    • Navon, A.1    Goldberg, A.L.2
  • 39
    • 0037022303 scopus 로고    scopus 로고
    • Functional p53 chimeras containing the Epstein-Barr virus Gly-Ala repeat are protected from Mdm2- and HPV-E6-induced proteolysis
    • Heessen, S., Leonchiks, A., Issaeva, N., Sharipo, A., Selivanova, G., Masucci, M.G. and Dantuma, N.P. (2002) Functional p53 chimeras containing the Epstein-Barr virus Gly-Ala repeat are protected from Mdm2- and HPV-E6-induced proteolysis. Proc. Natl. Acad. Sci. USA, 99, 1532-1537.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 1532-1537
    • Heessen, S.1    Leonchiks, A.2    Issaeva, N.3    Sharipo, A.4    Selivanova, G.5    Masucci, M.G.6    Dantuma, N.P.7
  • 40
    • 0032437713 scopus 로고    scopus 로고
    • Random coil conformation of a Gly/Ala-rich insert in IκB-α excludes structural stabilization as the mechanism for protection against proteasomal degradation
    • Leonchiks, A., Liepinsh, E., Barishev, M., Sharipo, A., Masucci, M.G. and Otting, G. (1998) Random coil conformation of a Gly/Ala-rich insert in IκB-α excludes structural stabilization as the mechanism for protection against proteasomal degradation. FEBS Lett., 440, 365-369.
    • (1998) FEBS Lett , vol.440 , pp. 365-369
    • Leonchiks, A.1    Liepinsh, E.2    Barishev, M.3    Sharipo, A.4    Masucci, M.G.5    Otting, G.6
  • 41
    • 18444386197 scopus 로고    scopus 로고
    • A long CAG repeat in the mouse Scal locus replicates SCA1 features and reveals the impact of protein solubility on selective neurodegeneration
    • Watase, K., Weeber, E.J., Xu, B., Antalffy, B., Yuva-Paylor, L., Hashimoto, K., Kano, M., Atkinson, R., Sun, Y., Armstrong, D.L. et al. (2002) A long CAG repeat in the mouse Scal locus replicates SCA1 features and reveals the impact of protein solubility on selective neurodegeneration. Neuron, 34, 905-919.
    • (2002) Neuron , vol.34 , pp. 905-919
    • Watase, K.1    Weeber, E.J.2    Xu, B.3    Antalffy, B.4    Yuva-Paylor, L.5    Hashimoto, K.6    Kano, M.7    Atkinson, R.8    Sun, Y.9    Armstrong, D.L.10
  • 42
    • 0032517816 scopus 로고    scopus 로고
    • Recruitment and the role of nuclear localization in polyglutamine-mediated aggregation
    • Perez, M.K., Paulson, H.L., Pendse, S.J., Saionz, S.J., Bonini, N.M. and Pittman, R.N. (1998) Recruitment and the role of nuclear localization in polyglutamine-mediated aggregation. J. Cell Biol., 143, 1457-1470.
    • (1998) J. Cell Biol , vol.143 , pp. 1457-1470
    • Perez, M.K.1    Paulson, H.L.2    Pendse, S.J.3    Saionz, S.J.4    Bonini, N.M.5    Pittman, R.N.6
  • 44
    • 0033638333 scopus 로고    scopus 로고
    • Harnessing the ubiquitination machinery to target the degradation of specific cellular proteins
    • Zhou, R, Bogacki, R., McReynolds, L. and Howley, P.M. (2000) Harnessing the ubiquitination machinery to target the degradation of specific cellular proteins. Mol. Cell, 6, 751-756.
    • (2000) Mol. Cell , vol.6 , pp. 751-756
    • Zhou, R.1    Bogacki, R.2    McReynolds, L.3    Howley, P.M.4
  • 45
    • 0035902475 scopus 로고    scopus 로고
    • Protacs: Chimeric molecules that target proteins to the Skp1-Cullin-F box complex for ubiquitination and degradation
    • Sakamoto, K.M., Kim, K.B., Kumagai, A., Mercurio, F., Crews, C.M. and Deshaies, R.J. (2001) Protacs: chimeric molecules that target proteins to the Skp1-Cullin-F box complex for ubiquitination and degradation. Proc. Natl. Acad. Sci. USA, 98, 8554-8559.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 8554-8559
    • Sakamoto, K.M.1    Kim, K.B.2    Kumagai, A.3    Mercurio, F.4    Crews, C.M.5    Deshaies, R.J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.