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Volumn 134, Issue 5, 2011, Pages 1400-1415

Overexpression of the autophagic beclin-1 protein clears mutant ataxin-3 and alleviates Machado-Joseph disease

Author keywords

ataxin 3; autophagy; beclin 1; Machado Joseph disease; neuroprotection

Indexed keywords

ATAXIN 3; BECLIN 1;

EID: 79957458183     PISSN: 00068950     EISSN: 14602156     Source Type: Journal    
DOI: 10.1093/brain/awr047     Document Type: Article
Times cited : (170)

References (48)
  • 1
    • 54449095083 scopus 로고    scopus 로고
    • Allele-specific RNA silencing of mutant ataxin-3 mediates neuroprotection in a rat model of Machado-Joseph disease
    • Alves S, Nascimento-Ferreira I, Auregan G, Hassig R, Dufour N, Brouillet E, et al. Allele-specific RNA silencing of mutant ataxin-3 mediates neuroprotection in a rat model of Machado-Joseph disease. PLoS One 2008a; 3: E3341.
    • (2008) PLoS One , vol.3
    • Alves, S.1    Nascimento-Ferreira, I.2    Auregan, G.3    Hassig, R.4    Dufour, N.5    Brouillet, E.6
  • 3
    • 19444382327 scopus 로고    scopus 로고
    • The dynamics of autophagy visualized in live cells: From autophagosome formation to fusion with endo/lysosomes
    • Bampton ET, Goemans CG, Niranjan D, Mizushima N, Tolkovsky AM. The dynamics of autophagy visualized in live cells: From autophagosome formation to fusion with endo/lysosomes. Autophagy 2005; 1: 23-36.
    • (2005) Autophagy , vol.1 , pp. 23-36
    • Bampton, E.T.1    Goemans, C.G.2    Niranjan, D.3    Mizushima, N.4    Tolkovsky, A.M.5
  • 4
    • 27944504351 scopus 로고    scopus 로고
    • P62/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtin-induced cell death
    • DOI 10.1083/jcb.200507002
    • Bjorkoy G, Lamark T, Brech A, Outzen H, Perander M, Overvatn A, et al. p62/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtin-induced cell death. J Cell Biol 2005; 171: 603-14. (Pubitemid 41668720)
    • (2005) Journal of Cell Biology , vol.171 , Issue.4 , pp. 603-614
    • Bjorkoy, G.1    Lamark, T.2    Brech, A.3    Outzen, H.4    Perander, M.5    Overvatn, A.6    Stenmark, H.7    Johansen, T.8
  • 5
    • 49049096562 scopus 로고    scopus 로고
    • Autophagy induction and autophagosome clearance in neurons: Relationship to autophagic pathology in Alzheimer's disease
    • Boland B, Kumar A, Lee S, Platt FM, Wegiel J, Yu WH, et al. Autophagy induction and autophagosome clearance in neurons: Relationship to autophagic pathology in Alzheimer's disease. J Neurosci 2008; 28: 6926-37.
    • (2008) J Neurosci , vol.28 , pp. 6926-6937
    • Boland, B.1    Kumar, A.2    Lee, S.3    Platt, F.M.4    Wegiel, J.5    Yu, W.H.6
  • 6
    • 35348886043 scopus 로고    scopus 로고
    • Physiological functions of Atg6/Beclin 1: A unique autophagy-related protein
    • DOI 10.1038/cr.2007.78, PII CR200778
    • Cao Y, Klionsky DJ. Physiological functions of Atg6/Beclin 1: A unique autophagy-related protein. Cell Res 2007; 17: 839-49. (Pubitemid 47585112)
    • (2007) Cell Research , vol.17 , Issue.10 , pp. 839-849
    • Cao, Y.1    Klionsky, D.J.2
  • 7
    • 0942287194 scopus 로고    scopus 로고
    • Poly-ubiquitin binding by the polyglutamine disease protein ataxin-3 links its normal function to protein surveillance pathways
    • DOI 10.1074/jbc.M310939200
    • Chai Y, Berke SS, Cohen RE, Paulson HL. Poly-ubiquitin binding by the polyglutamine disease protein ataxin-3 links its normal function to protein surveillance pathways. J Biol Chem 2004; 279: 3605-11. (Pubitemid 38140601)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.5 , pp. 3605-3611
    • Chai, Y.1    Berke, S.S.2    Cohen, R.E.3    Paulson, H.L.4
  • 8
    • 77949504405 scopus 로고    scopus 로고
    • Selective molecular alterations in the autophagy pathway in patients with Lewy body disease and in models of alphasynucleinopathy
    • Crews L, Spencer B, Desplats P, Patrick C, Paulino A, Rockenstein E, et al. Selective molecular alterations in the autophagy pathway in patients with Lewy body disease and in models of alphasynucleinopathy. PLoS One 2010; 5: E9313.
    • (2010) PLoS One , vol.5
    • Crews, L.1    Spencer, B.2    Desplats, P.3    Patrick, C.4    Paulino, A.5    Rockenstein, E.6
  • 9
    • 0442323561 scopus 로고    scopus 로고
    • Autophagy: In sickness and in health
    • DOI 10.1016/j.tcb.2003.12.002
    • Cuervo AM. Autophagy: In sickness and in health. Trends Cell Biol 2004; 14: 70-7. (Pubitemid 38186640)
    • (2004) Trends in Cell Biology , vol.14 , Issue.2 , pp. 70-77
    • Cuervo, A.M.1
  • 10
    • 0036580677 scopus 로고    scopus 로고
    • Lentiviral-Mediated Delivery of Mutant Huntingtin in the Striatum of Rats Induces a Selective Neuropathology Modulated by Polyglutamine Repeat Size, Huntingtin Expression Levels, and Protein Length
    • de Almeida LP, Ross CA, Zala D, Aebischer P, Deglon N. Lentiviralmediated delivery of mutant huntingtin in the striatum of rats induces a selective neuropathology modulated by polyglutamine repeat size, huntingtin expression levels, and protein length. J Neurosci 2002; 22: 3473-83. (Pubitemid 37465753)
    • (2002) Journal of Neuroscience , vol.22 , Issue.9 , pp. 3473-3483
    • De Almeida, L.P.1    Ross, C.A.2    Zala, D.3    Aebischer, P.4    Deglon, N.5
  • 12
    • 0042691818 scopus 로고    scopus 로고
    • Ataxin-3 interactions with Rad23 and valosin-containing protein and its associations with ubiquitin chains and the proteasome are consistent with a role in ubiquitin-mediated proteolysis
    • DOI 10.1128/MCB.23.18.6469-6483.2003
    • Doss-Pepe EW, Stenroos ES, Johnson WG, Madura K. Ataxin-3 interactions with rad23 and valosin-containing protein and its associations with ubiquitin chains and the proteasome are consistent with a role in ubiquitin-mediated proteolysis. Mol Cell Biol 2003; 23: 6469-83. (Pubitemid 37075759)
    • (2003) Molecular and Cellular Biology , vol.23 , Issue.18 , pp. 6469-6483
    • Doss-Pepe, E.W.1    Stenroos, E.S.2    Johnson, W.G.3    Madura, K.4
  • 13
    • 33745088678 scopus 로고    scopus 로고
    • Molecular pathogenesis of spinocerebellar ataxias
    • DOI 10.1093/brain/awl081
    • Duenas AM, Goold R, Giunti P. Molecular pathogenesis of spinocerebellar ataxias. Brain 2006; 129: 1357-70. (Pubitemid 43999370)
    • (2006) Brain , vol.129 , Issue.6 , pp. 1357-1370
    • Duenas, A.M.1    Goold, R.2    Giunti, P.3
  • 15
    • 33745192802 scopus 로고    scopus 로고
    • Suppression of basal autophagy in neural cells causes neurodegenerative disease in mice
    • Hara T, Nakamura K, Matsui M, Yamamoto A, Nakahara Y, Suzuki-Migishima R, et al. Suppression of basal autophagy in neural cells causes neurodegenerative disease in mice. Nature 2006; 441: 885-9.
    • (2006) Nature , vol.441 , pp. 885-889
    • Hara, T.1    Nakamura, K.2    Matsui, M.3    Yamamoto, A.4    Nakahara, Y.5    Suzuki-Migishima, R.6
  • 16
    • 79953153831 scopus 로고    scopus 로고
    • Selective degradation of p62 by autophagy
    • Ichimura Y, Komatsu M. Selective degradation of p62 by autophagy. Semin Immunopathol 2010; 32: 431-6.
    • (2010) Semin Immunopathol , vol.32 , pp. 431-436
    • Ichimura, Y.1    Komatsu, M.2
  • 18
    • 33846210657 scopus 로고    scopus 로고
    • Autophagy genes protect against disease caused by polyglutamine expansion proteins in Caenorhabditis elegans
    • Jia K, Hart AC, Levine B. Autophagy genes protect against disease caused by polyglutamine expansion proteins in Caenorhabditis elegans. Autophagy 2007; 3: 21-5. (Pubitemid 46100705)
    • (2007) Autophagy , vol.3 , Issue.1 , pp. 21-25
    • Jia, K.1    Hart, A.C.2    Levine, B.3
  • 19
    • 0034329418 scopus 로고    scopus 로고
    • Light chain 3, a mammalian homologue of yeast Apg8p, is localized in autophagosome membranes after processing
    • Kabeya Y, Mizushima N, Ueno T, Yamamoto A, Kirisako T, Noda T, et al. Light chain 3, a mammalian homologue of yeast Apg8p, is localized in autophagosome membranes after processing. EMBO J 2000; 19: 5720-8.
    • (2000) EMBO J , vol.19 , pp. 5720-5728
    • Kabeya, Y.1    Mizushima, N.2    Ueno, T.3    Yamamoto, A.4    Kirisako, T.5    Noda, T.6
  • 21
    • 0034307476 scopus 로고    scopus 로고
    • Huntingtin expression stimulates endosomal-lysosomal activity, endosome tubulation, and autophagy
    • Kegel KB, Kim M, Sapp E, McIntyre C, Castano JG, Aronin N, et al. Huntingtin expression stimulates endosomal-lysosomal activity, endosome tubulation, and autophagy. J Neurosci 2000; 20: 7268-78.
    • (2000) J Neurosci , vol.20 , pp. 7268-7278
    • Kegel, K.B.1    Kim, M.2    Sapp, E.3    McIntyre, C.4    Castano, J.G.5    Aronin, N.6
  • 22
    • 41149159767 scopus 로고    scopus 로고
    • Rapamycin inhibits polyglutamine aggregation independently of autophagy by reducing protein synthesis
    • DOI 10.1124/mol.107.043398
    • King MA, Hands S, Hafiz F, Mizushima N, Tolkovsky AM, Wyttenbach A. Rapamycin inhibits polyglutamine aggregation independently of autophagy by reducing protein synthesis. Mol Pharmacol 2008; 73: 1052-63. (Pubitemid 351439187)
    • (2008) Molecular Pharmacology , vol.73 , Issue.4 , pp. 1052-1063
    • King, M.A.1    Hands, S.2    Hafiz, F.3    Mizushima, N.4    Tolkovsky, A.M.5    Wyttenbach, A.6
  • 23
    • 65549142204 scopus 로고    scopus 로고
    • A role for ubiquitin in selective autophagy
    • Kirkin V, McEwan DG, Novak I, Dikic I. A role for ubiquitin in selective autophagy. Mol Cell 2009; 34: 259-69.
    • (2009) Mol Cell , vol.34 , pp. 259-269
    • Kirkin, V.1    McEwan, D.G.2    Novak, I.3    Dikic, I.4
  • 24
    • 33646800306 scopus 로고    scopus 로고
    • Loss of autophagy in the central nervous system causes neurodegeneration in mice
    • Komatsu M, Waguri S, Chiba T, Murata S, Iwata J, Tanida I, et al. Loss of autophagy in the central nervous system causes neurodegeneration in mice. Nature 2006; 441: 880-4.
    • (2006) Nature , vol.441 , pp. 880-884
    • Komatsu, M.1    Waguri, S.2    Chiba, T.3    Murata, S.4    Iwata, J.5    Tanida, I.6
  • 26
    • 53749088439 scopus 로고    scopus 로고
    • Intracellular degradation of misfolded proteins in polyglutamine neurodegenerative diseases
    • Li X, Li H, Li XJ. Intracellular degradation of misfolded proteins in polyglutamine neurodegenerative diseases. Brain Res Rev 2008; 59: 245-52.
    • (2008) Brain Res Rev , vol.59 , pp. 245-252
    • Li, X.1    Li, H.2    Li, X.J.3
  • 28
    • 74249103961 scopus 로고    scopus 로고
    • Autophagy induction reduces mutant ataxin-3 levels and toxicity in a mouse model of spinocerebellar ataxia type 3
    • Menzies FM, Huebener J, Renna M, Bonin M, Riess O, Rubinsztein DC. Autophagy induction reduces mutant ataxin-3 levels and toxicity in a mouse model of spinocerebellar ataxia type 3. Brain 2009; 133: 93-104.
    • (2009) Brain , vol.133 , pp. 93-104
    • Menzies, F.M.1    Huebener, J.2    Renna, M.3    Bonin, M.4    Riess, O.5    Rubinsztein, D.C.6
  • 29
    • 75749122303 scopus 로고    scopus 로고
    • Methods in mammalian autophagy research
    • Mizushima N, Yoshimori T, Levine B. Methods in mammalian autophagy research. Cell 2010; 140: 313-26.
    • (2010) Cell , Issue.140 , pp. 313-326
    • Mizushima, N.1    Yoshimori, T.2    Levine, B.3
  • 33
    • 33750363298 scopus 로고    scopus 로고
    • The roles of intracellular protein-degradation pathways in neurodegeneration
    • DOI 10.1038/nature05291, PII NATURE05291
    • Rubinsztein DC. The roles of intracellular protein-degradation pathways in neurodegeneration. Nature 2006; 443: 780-6. (Pubitemid 44622682)
    • (2006) Nature , vol.443 , Issue.7113 , pp. 780-786
    • Rubinsztein, D.C.1
  • 36
    • 46849121421 scopus 로고    scopus 로고
    • Utilizing flow cytometry to monitor autophagy in living mammalian cells
    • Shvets E, Fass E, Elazar Z. Utilizing flow cytometry to monitor autophagy in living mammalian cells. Autophagy 2008; 4: 621-8.
    • (2008) Autophagy , vol.4 , pp. 621-628
    • Shvets, E.1    Fass, E.2    Elazar, Z.3
  • 37
    • 38949099761 scopus 로고    scopus 로고
    • Promoting basal levels of autophagy in the nervous system enhances longevity and oxidant resistance in adult Drosophila
    • Simonsen A, Cumming RC, Brech A, Isakson P, Schubert DR, Finley KD. Enhanced neuronal autophagy promotes longevity and oxidant resistance in drosophila. Autophagy 2008; 4: 176-84. (Pubitemid 351231181)
    • (2008) Autophagy , vol.4 , Issue.2 , pp. 176-184
    • Simonsen, A.1    Cumming, R.C.2    Brech, A.3    Isakson, P.4    Schubert, D.R.5    Finley, K.D.6
  • 38
    • 70350550208 scopus 로고    scopus 로고
    • Beclin 1 gene transfer activates autophagy and ameliorates the neurodegenerative pathology in alpha-synuclein models of Parkinson's and Lewy body diseases
    • Spencer B, Potkar R, Trejo M, Rockenstein E, Patrick C, Gindi R, et al. Beclin 1 gene transfer activates autophagy and ameliorates the neurodegenerative pathology in alpha-synuclein models of Parkinson's and Lewy body diseases. J Neurosci 2009; 29: 13578-88.
    • (2009) J Neurosci , vol.29 , pp. 13578-13588
    • Spencer, B.1    Potkar, R.2    Trejo, M.3    Rockenstein, E.4    Patrick, C.5    Gindi, R.6
  • 40
    • 57649234905 scopus 로고    scopus 로고
    • Autophagy genes and ageing
    • Vellai T. Autophagy genes and ageing. Cell Death Differ 2009; 16: 94-102.
    • (2009) Cell Death Differ , vol.16 , pp. 94-102
    • Vellai, T.1
  • 42
    • 77954116814 scopus 로고    scopus 로고
    • Autophagy gone awry in neurodegenerative diseases
    • Wong E, Cuervo AM. Autophagy gone awry in neurodegenerative diseases. Nat Neurosci 2010; 13: 805-11.
    • (2010) Nat Neurosci , vol.13 , pp. 805-811
    • Wong, E.1    Cuervo, A.M.2
  • 43
    • 32044465506 scopus 로고    scopus 로고
    • TOR signaling in growth and metabolism
    • DOI 10.1016/j.cell.2006.01.016, PII S0092867406001085
    • Wullschleger S, Loewith R, Hall MN. TOR signaling in growth and metabolism. Cell 2006; 124: 471-84. (Pubitemid 43199434)
    • (2006) Cell , vol.124 , Issue.3 , pp. 471-484
    • Wullschleger, S.1    Loewith, R.2    Hall, M.N.3
  • 44
    • 27644484061 scopus 로고    scopus 로고
    • Autophagy: Molecular machinery for self-eating
    • DOI 10.1038/sj.cdd.4401765, PII 4401765
    • Yorimitsu T, Klionsky DJ. Autophagy: Molecular machinery for self-eating. Cell Death Differ 2005; 12 (Suppl 2): 1542-52. (Pubitemid 41553991)
    • (2005) Cell Death and Differentiation , vol.12 , Issue.SUPPL. 2 , pp. 1542-1552
    • Yorimitsu, T.1    Klionsky, D.J.2
  • 46
    • 27744443276 scopus 로고    scopus 로고
    • Progressive and selective striatal degeneration in primary neuronal cultures using lentiviral vector coding for a mutant huntingtin fragment
    • DOI 10.1016/j.nbd.2005.05.017, PII S096999610500149X
    • Zala D, Benchoua A, Brouillet E, Perrin V, Gaillard MC, Zurn AD, et al. Progressive and selective striatal degeneration in primary neuronal cultures using lentiviral vector coding for a mutant huntingtin fragment. Neurobiol Dis 2005; 20: 785-98. (Pubitemid 41622214)
    • (2005) Neurobiology of Disease , vol.20 , Issue.3 , pp. 785-798
    • Zala, D.1    Benchoua, A.2    Brouillet, E.3    Perrin, V.4    Gaillard, M.-C.5    Zurn, A.D.6    Aebischer, P.7    Deglon, N.8
  • 47
    • 32244442749 scopus 로고    scopus 로고
    • Functional specificity of the mammalian Beclin-Vps34 PI 3-kinase complex in macroautophagy versus endocytosis and lysosomal enzyme trafficking
    • DOI 10.1242/jcs.02735
    • Zeng X, Overmeyer JH, Maltese WA. Functional specificity of the mammalian Beclin-Vps34 PI 3-kinase complex in macroautophagy versus endocytosis and lysosomal enzyme trafficking. J Cell Sci 2006; 119: 259-70. (Pubitemid 43210695)
    • (2006) Journal of Cell Science , vol.119 , Issue.2 , pp. 259-270
    • Zeng, X.1    Overmeyer, J.H.2    Maltese, W.A.3
  • 48
    • 0033760073 scopus 로고    scopus 로고
    • Spinocerebellar ataxias
    • Zoghbi HY. Spinocerebellar ataxias. Neurobiol Dis 2000; 7: 523-7.
    • (2000) Neurobiol Dis , vol.7 , pp. 523-527
    • Zoghbi, H.Y.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.