메뉴 건너뛰기




Volumn 15, Issue 6, 2006, Pages 1025-1041

Suppression of polyglutamine-induced toxicity in cell and animal models of Huntington's disease by ubiquilin

Author keywords

[No Author keywords available]

Indexed keywords

CASPASE; DNA; GREEN FLUORESCENT PROTEIN; HUNTINGTIN; HYBRID PROTEIN; NERVE PROTEIN; POLYGLUTAMINE; UBIQUILIN 1; UNCLASSIFIED DRUG;

EID: 33644771265     PISSN: 09646906     EISSN: 14602083     Source Type: Journal    
DOI: 10.1093/hmg/ddl017     Document Type: Article
Times cited : (101)

References (48)
  • 2
    • 0027480960 scopus 로고
    • A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes
    • The Huntington's Disease Collaborative Research Group
    • The Huntington's Disease Collaborative Research Group. (1993) A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes. Cell, 72, 971-983.
    • (1993) Cell , vol.72 , pp. 971-983
  • 3
    • 8844220536 scopus 로고    scopus 로고
    • Huntingtin and the molecular pathogenesis of Huntington's disease. Fourth in molecular medicine review series
    • Landles, C. and Bates, G.P. (2004) Huntingtin and the molecular pathogenesis of Huntington's disease. Fourth in molecular medicine review series. EMBO Rep., 5, 958-963.
    • (2004) EMBO Rep. , vol.5 , pp. 958-963
    • Landles, C.1    Bates, G.P.2
  • 4
    • 0141891215 scopus 로고    scopus 로고
    • Pathogenesis of polyglutamine disorders: Aggregation revisited
    • (Spec No. 2)
    • Michalik, A. and Van Broeckhoven, C. (2003) Pathogenesis of polyglutamine disorders: Aggregation revisited. Hum. Mol. Genet., 12 (Spec No. 2), R173-R186.
    • (2003) Hum. Mol. Genet. , vol.12
    • Michalik, A.1    Van Broeckhoven, C.2
  • 5
    • 0038521282 scopus 로고    scopus 로고
    • Polyglutamines placed into context
    • La Spada, A.R. and Taylor, J.P. (2003) Polyglutamines placed into context. Neuron, 38, 681-684.
    • (2003) Neuron , vol.38 , pp. 681-684
    • La Spada, A.R.1    Taylor, J.P.2
  • 6
    • 0037194897 scopus 로고    scopus 로고
    • Polyglutamine pathogenesis: Emergence of unifying mechanisms for Huntington's disease and related disorders
    • Ross, C.A. (2002) Polyglutamine pathogenesis: Emergence of unifying mechanisms for Huntington's disease and related disorders. Neuron, 35, 819-822.
    • (2002) Neuron , vol.35 , pp. 819-822
    • Ross, C.A.1
  • 7
    • 3142514201 scopus 로고    scopus 로고
    • Protein aggregation and neurodegenerative disease
    • Ross, C.A. and Poirier, M.A. (2004) Protein aggregation and neurodegenerative disease. Nat. Med., 10 (suppl.), S10-S17.
    • (2004) Nat. Med. , vol.10 , Issue.SUPPL.
    • Ross, C.A.1    Poirier, M.A.2
  • 8
    • 7244236320 scopus 로고    scopus 로고
    • Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death
    • Arrasate, M., Mitra, S., Schweitzer, E.S., Segal, M.R. and Finkbeiner, S. (2004) Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death. Nature, 431, 805-810.
    • (2004) Nature , vol.431 , pp. 805-810
    • Arrasate, M.1    Mitra, S.2    Schweitzer, E.S.3    Segal, M.R.4    Finkbeiner, S.5
  • 9
    • 14644419638 scopus 로고    scopus 로고
    • Neuronal dysfunction in a polyglutamine disease model occurs in the absence of ubiquitin-proteasome system impairment and inversely correlates with the degree of nuclear inclusion formation
    • Bowman, A.B., Yoo, S.Y., Dantuma, N.P. and Zoghbi, H.Y. (2005) Neuronal dysfunction in a polyglutamine disease model occurs in the absence of ubiquitin-proteasome system impairment and inversely correlates with the degree of nuclear inclusion formation. Hum. Mol. Genet., 14, 679-691.
    • (2005) Hum. Mol. Genet. , vol.14 , pp. 679-691
    • Bowman, A.B.1    Yoo, S.Y.2    Dantuma, N.P.3    Zoghbi, H.Y.4
  • 11
    • 0034645063 scopus 로고    scopus 로고
    • Identification of ubiquilin, a novel presenilin interactor that increases presenilin protein accumulation
    • Mah, A.L., Perry, G., Smith, M.A. and Monteiro, M.J. (2000) Identification of ubiquilin, a novel presenilin interactor that increases presenilin protein accumulation. J. Cell Biol., 151, 847-862.
    • (2000) J. Cell Biol. , vol.151 , pp. 847-862
    • Mah, A.L.1    Perry, G.2    Smith, M.A.3    Monteiro, M.J.4
  • 12
    • 0034703397 scopus 로고    scopus 로고
    • Identification and characterization of an ataxin-1-interacting protein: A1Up, a ubiquitin-like nuclear protein
    • Davidson, J.D., Riley, B., Burright, E.N., Duvick, L.A., Zoghbi, H.Y. and Orr, H.T. (2000) Identification and characterization of an ataxin-1-interacting protein: A1Up, a ubiquitin-like nuclear protein. Hum. Mol. Genet., 9, 2305-2312.
    • (2000) Hum. Mol. Genet. , vol.9 , pp. 2305-2312
    • Davidson, J.D.1    Riley, B.2    Burright, E.N.3    Duvick, L.A.4    Zoghbi, H.Y.5    Orr, H.T.6
  • 13
    • 3342879140 scopus 로고    scopus 로고
    • Identification of ubiquitin-interacting proteins in purified polyglutamine aggregates
    • Doi, H., Mitsui, K., Kurosawa, M., Machida, Y., Kuroiwa, Y. and Nukina, N. (2004) Identification of ubiquitin-interacting proteins in purified polyglutamine aggregates. FEBS Lett., 571, 171-176.
    • (2004) FEBS Lett. , vol.571 , pp. 171-176
    • Doi, H.1    Mitsui, K.2    Kurosawa, M.3    Machida, Y.4    Kuroiwa, Y.5    Nukina, N.6
  • 15
    • 0036566675 scopus 로고    scopus 로고
    • Heat shock protein 27 prevents cellular polyglutamine toxicity and suppresses the increase of reactive oxygen species caused by huntingtin
    • Wyttenbach, A., Sauvageot, O., Carmichael, J., Diaz-Latoud, C., Arrigo, A.P. and Rubinsztein, D.C. (2002) Heat shock protein 27 prevents cellular polyglutamine toxicity and suppresses the increase of reactive oxygen species caused by huntingtin. Hum. Mol. Genet., 11, 1137-1151.
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 1137-1151
    • Wyttenbach, A.1    Sauvageot, O.2    Carmichael, J.3    Diaz-Latoud, C.4    Arrigo, A.P.5    Rubinsztein, D.C.6
  • 16
    • 0029940901 scopus 로고    scopus 로고
    • Removal of serum from primary cultures of cerebellar granule neurons induces oxidative stress and DNA fragmentation: Protection with antioxidants and glutamate receptor antagonists
    • Atabay, C., Cagnoli, C.M., Kharlamov, E., Ikonomovic, M.D. and Manev, H. (1996) Removal of serum from primary cultures of cerebellar granule neurons induces oxidative stress and DNA fragmentation: Protection with antioxidants and glutamate receptor antagonists. J. Neurosci. Res., 43, 465-475.
    • (1996) J. Neurosci. Res. , vol.43 , pp. 465-475
    • Atabay, C.1    Cagnoli, C.M.2    Kharlamov, E.3    Ikonomovic, M.D.4    Manev, H.5
  • 17
    • 0030843476 scopus 로고    scopus 로고
    • Melatonin rescues dopamine neurons from cell death in tissue culture models of oxidative stress
    • Iacovitti, L., Stull, N.D. and Johnston, K. (1997) Melatonin rescues dopamine neurons from cell death in tissue culture models of oxidative stress. Brain Res., 768, 317-326.
    • (1997) Brain Res. , vol.768 , pp. 317-326
    • Iacovitti, L.1    Stull, N.D.2    Johnston, K.3
  • 18
    • 0037155817 scopus 로고    scopus 로고
    • The roles of thioredoxin in protection against oxidative stress-induced apoptosis in SH-SY5Y cells
    • Andoh, T., Chock, P.B. and Chiueh, C.C. (2002) The roles of thioredoxin in protection against oxidative stress-induced apoptosis in SH-SY5Y cells. J. Biol. Chem., 277, 9655-9660.
    • (2002) J. Biol. Chem. , vol.277 , pp. 9655-9660
    • Andoh, T.1    Chock, P.B.2    Chiueh, C.C.3
  • 19
    • 0141927326 scopus 로고    scopus 로고
    • Oxidative stress and activation of proteasome protease during serum deprivation-induced apoptosis in rat hepatoma cells; inhibition of cell death by melatonin
    • Pandey, S., Lopez, C. and Jammu, A. (2003) Oxidative stress and activation of proteasome protease during serum deprivation-induced apoptosis in rat hepatoma cells; inhibition of cell death by melatonin. Apoptosis, 8, 497-508.
    • (2003) Apoptosis , vol.8 , pp. 497-508
    • Pandey, S.1    Lopez, C.2    Jammu, A.3
  • 20
    • 1842861767 scopus 로고    scopus 로고
    • Hypoxia and CoCl2 protect HepG2 cells against serum deprivation- and t-BHP-induced apoptosis: A possible anti-apoptotic role for HIF-1
    • Piret, J.P., Lecocq, C., Toffoli, S., Ninane, N., Raes, M. and Michiels, C. (2004) Hypoxia and CoCl2 protect HepG2 cells against serum deprivation- and t-BHP-induced apoptosis: A possible anti-apoptotic role for HIF-1. Exp. Cell Res., 295, 340-349.
    • (2004) Exp. Cell Res. , vol.295 , pp. 340-349
    • Piret, J.P.1    Lecocq, C.2    Toffoli, S.3    Ninane, N.4    Raes, M.5    Michiels, C.6
  • 22
    • 0032879437 scopus 로고    scopus 로고
    • Membrane filter assay for detection of amyloid-like polyglutamine-containing protein aggregates
    • Wanker, E.E., Scherzinger, E., Heiser, V., Sittler, A., Eickhoff, H. and Lehrach, H. (1999) Membrane filter assay for detection of amyloid-like polyglutamine-containing protein aggregates. Methods Enzymol., 309, 375-386.
    • (1999) Methods Enzymol. , vol.309 , pp. 375-386
    • Wanker, E.E.1    Scherzinger, E.2    Heiser, V.3    Sittler, A.4    Eickhoff, H.5    Lehrach, H.6
  • 23
    • 27744468749 scopus 로고    scopus 로고
    • Ubiquilin regulates presenilin endoproteolysis and modulates gamma-secretase components, Pen-2 and Nicastrin
    • Massey, L.K., Mah, A.L. and Monteiro, M.J. (2005) Ubiquilin regulates presenilin endoproteolysis and modulates gamma-secretase components, Pen-2 and Nicastrin. Biochem. J., 391, 513-525.
    • (2005) Biochem. J. , vol.391 , pp. 513-525
    • Massey, L.K.1    Mah, A.L.2    Monteiro, M.J.3
  • 25
    • 0036678146 scopus 로고    scopus 로고
    • The threshold for polyglutamine-expansion protein aggregation and cellular toxicity is dynamic and influenced by aging in Caenorhabditis elegans
    • Morley, J.F., Brignull, H.R., Weyers, J.J. and Morimoto, R.I. (2002) The threshold for polyglutamine-expansion protein aggregation and cellular toxicity is dynamic and influenced by aging in Caenorhabditis elegans. Proc. Natl Acad. Sci. USA, 99, 10417-10422.
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 10417-10422
    • Morley, J.F.1    Brignull, H.R.2    Weyers, J.J.3    Morimoto, R.I.4
  • 26
    • 0037319121 scopus 로고    scopus 로고
    • Suppression of polyglutamine-induced protein aggregation in Caenorhabditis elegans by torsin proteins
    • Caldwell, G.A., Cao, S., Sexton, E.G., Gelwix, C.C., Bevel, J.P. and Caldwell, K.A. (2003) Suppression of polyglutamine-induced protein aggregation in Caenorhabditis elegans by torsin proteins. Hum. Mol. Genet., 12, 307-319.
    • (2003) Hum. Mol. Genet. , vol.12 , pp. 307-319
    • Caldwell, G.A.1    Cao, S.2    Sexton, E.G.3    Gelwix, C.C.4    Bevel, J.P.5    Caldwell, K.A.6
  • 27
    • 1642340527 scopus 로고    scopus 로고
    • Analysis of the two p97/VCP/Cdc48p proteins of Caenorhabditis elegans and their suppression of polyglutamine-induced protein aggregation
    • Yamanaka, K., Okubo, Y., Suzaki, T. and Ogura, T. (2004) Analysis of the two p97/VCP/Cdc48p proteins of Caenorhabditis elegans and their suppression of polyglutamine-induced protein aggregation. J. Struct. Biol., 146, 242-250.
    • (2004) J. Struct. Biol. , vol.146 , pp. 242-250
    • Yamanaka, K.1    Okubo, Y.2    Suzaki, T.3    Ogura, T.4
  • 28
    • 0027451263 scopus 로고
    • Sequence requirements for myosin gene expression and regulation in Caenorhabditis elegans
    • Okkema, P.G., Harrison, S.W., Plunger, V., Aryana, A. and Fire, A. (1993) Sequence requirements for myosin gene expression and regulation in Caenorhabditis elegans. Genetics, 135, 385-404.
    • (1993) Genetics , vol.135 , pp. 385-404
    • Okkema, P.G.1    Harrison, S.W.2    Plunger, V.3    Aryana, A.4    Fire, A.5
  • 29
    • 0032578911 scopus 로고    scopus 로고
    • Specific interference by ingested dsRNA
    • Timmons, L. and Fire, A. (1998) Specific interference by ingested dsRNA. Nature, 395, 854.
    • (1998) Nature , vol.395 , pp. 854
    • Timmons, L.1    Fire, A.2
  • 30
    • 0035941485 scopus 로고    scopus 로고
    • Ingestion of bacterially expressed dsRNAs can produce specific and potent genetic interference in Caenorhabditis elegans
    • Timmons, L., Court, D.L. and Fire, A. (2001) Ingestion of bacterially expressed dsRNAs can produce specific and potent genetic interference in Caenorhabditis elegans. Gene, 263, 103-112.
    • (2001) Gene , vol.263 , pp. 103-112
    • Timmons, L.1    Court, D.L.2    Fire, A.3
  • 32
    • 3242695184 scopus 로고    scopus 로고
    • Progressive decrease in chaperone protein levels in a mouse model of Huntington's disease and induction of stress proteins as a therapeutic approach
    • Hay, D.G., Sathasivam, K., Tobaben, S., Stahl, B., Marber, M., Mestril, R., Mahal, A., Smith, D.L., Woodman, B. and Bates, G.P. (2004) Progressive decrease in chaperone protein levels in a mouse model of Huntington's disease and induction of stress proteins as a therapeutic approach. Hum. Mol. Genet., 13, 1389-1405.
    • (2004) Hum. Mol. Genet. , vol.13 , pp. 1389-1405
    • Hay, D.G.1    Sathasivam, K.2    Tobaben, S.3    Stahl, B.4    Marber, M.5    Mestril, R.6    Mahal, A.7    Smith, D.L.8    Woodman, B.9    Bates, G.P.10
  • 33
    • 20744441099 scopus 로고    scopus 로고
    • Modulation of prion-dependent polyglutamine aggregation and toxicity by chaperone proteins in the yeast model
    • Gokhale, K.C., Newnam, G.P., Sherman, M.Y. and Chernoff, Y.O. (2005) Modulation of prion-dependent polyglutamine aggregation and toxicity by chaperone proteins in the yeast model. J. Biol. Chem., 280, 22809-22818.
    • (2005) J. Biol. Chem. , vol.280 , pp. 22809-22818
    • Gokhale, K.C.1    Newnam, G.P.2    Sherman, M.Y.3    Chernoff, Y.O.4
  • 34
    • 20444378891 scopus 로고    scopus 로고
    • The unfolded protein response modulates toxicity of the expanded glutamine androgen receptor
    • Thomas, M., Yu, Z., Dadgar, N., Varambally, S., Yu, J., Chinnaiyan, A.M. and Lieberman, A.P. (2005) The unfolded protein response modulates toxicity of the expanded glutamine androgen receptor. J. Biol. Chem., 280, 21264-21271.
    • (2005) J. Biol. Chem. , vol.280 , pp. 21264-21271
    • Thomas, M.1    Yu, Z.2    Dadgar, N.3    Varambally, S.4    Yu, J.5    Chinnaiyan, A.M.6    Lieberman, A.P.7
  • 35
    • 0037059042 scopus 로고    scopus 로고
    • Molecular chaperones as modulators of polyglutamine protein aggregation and toxicity
    • Sakahira, H., Breuer, P., Hayer-Hartl, M.K. and Hartl, F.U. (2002) Molecular chaperones as modulators of polyglutamine protein aggregation and toxicity. Proc. Natl Acad. Sci. USA, 99(Suppl. 4), 16412-16418.
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , Issue.SUPPL. 4 , pp. 16412-16418
    • Sakahira, H.1    Breuer, P.2    Hayer-Hartl, M.K.3    Hartl, F.U.4
  • 36
    • 0141632772 scopus 로고    scopus 로고
    • The ubiquitin-associated domain of hPLIC-2 interacts with the proteasome
    • Kleijnen, M.F., Alarcon, R.M. and Howley, P.M. (2003) The ubiquitin-associated domain of hPLIC-2 interacts with the proteasome. Mol. Biol. Cell, 14, 3868-3875.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 3868-3875
    • Kleijnen, M.F.1    Alarcon, R.M.2    Howley, P.M.3
  • 38
    • 0036277299 scopus 로고    scopus 로고
    • Rad23 promotes the targeting of proteolytic substrates to the proteasome
    • Chen, L. and Madura, K. (2002) Rad23 promotes the targeting of proteolytic substrates to the proteasome. Mol. Cell. Biol., 22, 4902-4913.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 4902-4913
    • Chen, L.1    Madura, K.2
  • 39
    • 3042677641 scopus 로고    scopus 로고
    • Rad23 and Rpn10 serve as alternative ubiquitin receptors for the proteasome
    • Elsasser, S., Chandler-Militello, D., Muller, B., Hanna, J. and Finley, D. (2004) Rad23 and Rpn10 serve as alternative ubiquitin receptors for the proteasome. J. Biol. Chem., 279, 26817-26822.
    • (2004) J. Biol. Chem. , vol.279 , pp. 26817-26822
    • Elsasser, S.1    Chandler-Militello, D.2    Muller, B.3    Hanna, J.4    Finley, D.5
  • 40
    • 3142566639 scopus 로고    scopus 로고
    • Multiubiquitin chain receptors define a layer of substrate selectivity in the ubiquitin-proteasome system
    • Verma, R., Oania, R., Graumann, J. and Deshaies, R.J. (2004) Multiubiquitin chain receptors define a layer of substrate selectivity in the ubiquitin-proteasome system. Cell, 118, 99-110.
    • (2004) Cell , vol.118 , pp. 99-110
    • Verma, R.1    Oania, R.2    Graumann, J.3    Deshaies, R.J.4
  • 42
    • 0037144597 scopus 로고    scopus 로고
    • Role of ubiquilin associated with protein-disulfide isomerase in the endoplasmic reticulum in stress-induced apoptotic cell death
    • Ko, H.S., Uehara, T. and Nomura, Y. (2002) Role of ubiquilin associated with protein-disulfide isomerase in the endoplasmic reticulum in stress-induced apoptotic cell death. J. Biol. Chem., 277, 35386-35392.
    • (2002) J. Biol. Chem. , vol.277 , pp. 35386-35392
    • Ko, H.S.1    Uehara, T.2    Nomura, Y.3
  • 43
    • 21244487545 scopus 로고    scopus 로고
    • The ubiquilin 1 gene and Alzheimer's disease
    • author reply 2752-2753
    • Slifer, M.A., Martin, E.R., Haines, J.L. and Pericak-Vance, M.A. (2005) The ubiquilin 1 gene and Alzheimer's disease. N. Engl. J. Med., 352, 2752-2753; author reply 2752-2753.
    • (2005) N. Engl. J. Med. , vol.352 , pp. 2752-2753
    • Slifer, M.A.1    Martin, E.R.2    Haines, J.L.3    Pericak-Vance, M.A.4
  • 44
    • 33644611017 scopus 로고    scopus 로고
    • Genetic association of ubiquilin with Alzheimer's disease and related quantitative measures
    • November 22, 2005 advanced online [Epub ahead of print], doi: 10.1038/sj.4001775
    • Kamboh, M.I., Minster, R.L., Feingold, E. and Dekosky, S.T. (2005) Genetic association of ubiquilin with Alzheimer's disease and related quantitative measures. Mol. Psychiatry, November 22, 2005 advanced online [Epub ahead of print], doi: 10.1038/sj.4001775.
    • (2005) Mol. Psychiatry
    • Kamboh, M.I.1    Minster, R.L.2    Feingold, E.3    Dekosky, S.T.4
  • 47
    • 0016063911 scopus 로고
    • The genetics of Caenorhabditis elegans
    • Brenner, S. (1974) The genetics of Caenorhabditis elegans. Genetics, 77, 71-94.
    • (1974) Genetics , vol.77 , pp. 71-94
    • Brenner, S.1
  • 48


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.