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Volumn 39, Issue 3, 2007, Pages 373-379

Duplication of Atxn1l suppresses SCA1 neuropathology by decreasing incorporation of polyglutamine-expanded ataxin-1 into native complexes

Author keywords

[No Author keywords available]

Indexed keywords

ATAXIN 1; ATAXIN 1 LIKE PROTEIN; GENE PRODUCT; POLYGLUTAMINE; PROTEIN; UNCLASSIFIED DRUG;

EID: 33847290297     PISSN: 10614036     EISSN: 15461718     Source Type: Journal    
DOI: 10.1038/ng1977     Document Type: Article
Times cited : (66)

References (29)
  • 1
    • 23944438950 scopus 로고    scopus 로고
    • The AXH domain of Ataxin-1 mediates neurodegeneration through its interaction with Gfi-1/Senseless proteins
    • Tsuda, H. et al. The AXH domain of Ataxin-1 mediates neurodegeneration through its interaction with Gfi-1/Senseless proteins. Cell 122, 633-644 (2005).
    • (2005) Cell , vol.122 , pp. 633-644
    • Tsuda, H.1
  • 2
    • 1642447764 scopus 로고    scopus 로고
    • Ataxin 1, a SCA1 neurodegenerative disorder protein, is functionally linked to the silencing mediator of retinoid and thyroid hormone receptors
    • Tsai, C.C. et al. Ataxin 1, a SCA1 neurodegenerative disorder protein, is functionally linked to the silencing mediator of retinoid and thyroid hormone receptors. Proc. Natl. Acad. Sci. USA 101, 4047-4052 (2004).
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 4047-4052
    • Tsai, C.C.1
  • 3
    • 25144468986 scopus 로고    scopus 로고
    • Boat, an AXH domain protein, suppresses the cytotoxicity of mutant ataxin-1
    • Mizutani, A. et al. Boat, an AXH domain protein, suppresses the cytotoxicity of mutant ataxin-1. EMBO J. 24, 3339-3351 (2005).
    • (2005) EMBO J , vol.24 , pp. 3339-3351
    • Mizutani, A.1
  • 4
    • 33845657872 scopus 로고    scopus 로고
    • ATAXIN-1 interacts with the repressor Capicua in its native complex to cause SCA1 neuropathology
    • Lam, Y.C. et al. ATAXIN-1 interacts with the repressor Capicua in its native complex to cause SCA1 neuropathology. Cell 127, 1335-1347 (2006).
    • (2006) Cell , vol.127 , pp. 1335-1347
    • Lam, Y.C.1
  • 5
    • 0032528167 scopus 로고    scopus 로고
    • Mice lacking ataxin-1 display learning deficits and decreased hippocampal paired-pulse facilitation
    • Matilla, A. et al. Mice lacking ataxin-1 display learning deficits and decreased hippocampal paired-pulse facilitation. J. Neurosci. 18, 5508-5516 (1998).
    • (1998) J. Neurosci , vol.18 , pp. 5508-5516
    • Matilla, A.1
  • 6
    • 33646687963 scopus 로고    scopus 로고
    • A protein-protein interaction network for human inherited ataxias and disorders of Purkinje cell degeneration
    • Lim, J. et al. A protein-protein interaction network for human inherited ataxias and disorders of Purkinje cell degeneration. Cell 125, 801-814 (2006).
    • (2006) Cell , vol.125 , pp. 801-814
    • Lim, J.1
  • 7
    • 18444386197 scopus 로고    scopus 로고
    • A long CAG repeat in the mouse Sca1 locus replicates SCA1 features and reveals the impact of protein solubility on selective neurodegeneration
    • Watase, K. et al. A long CAG repeat in the mouse Sca1 locus replicates SCA1 features and reveals the impact of protein solubility on selective neurodegeneration. Neuron 34, 905-919 (2002).
    • (2002) Neuron , vol.34 , pp. 905-919
    • Watase, K.1
  • 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. & Finkbeiner, S. Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death. Nature 431, 805-810 (2004).
    • (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. & Zoghbi, H.Y. 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).
    • (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
  • 10
    • 23844472610 scopus 로고    scopus 로고
    • Absence of behavioral abnormalities and neurodegeneration in vivo despite widespread neuronal huntingtin inclusions
    • Slow, E.J. et al. Absence of behavioral abnormalities and neurodegeneration in vivo despite widespread neuronal huntingtin inclusions. Proc. Natl. Acad. Sci. USA 102, 11402-11407 (2005).
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 11402-11407
    • Slow, E.J.1
  • 11
    • 20044390015 scopus 로고    scopus 로고
    • A potent small molecule inhibits polyglutamine aggregation in Huntington's disease neurons and suppresses neurodegeneration in vivo
    • Zhang, X. et al. A potent small molecule inhibits polyglutamine aggregation in Huntington's disease neurons and suppresses neurodegeneration in vivo. Proc. Natl. Acad. Sci. USA 102, 892-897 (2005).
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 892-897
    • Zhang, X.1
  • 12
    • 33645235438 scopus 로고    scopus 로고
    • Pharmacological promotion of inclusion formation: A therapeutic approach for Huntington's and Parkinson's diseases
    • Bodner, R.A. et al. Pharmacological promotion of inclusion formation: a therapeutic approach for Huntington's and Parkinson's diseases. Proc. Natl. Acad. Sci. USA 103, 4246-4251 (2006).
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 4246-4251
    • Bodner, R.A.1
  • 13
    • 0037388418 scopus 로고    scopus 로고
    • Aggresomes protect cells by enhancing the degradation of toxic polyglutamine-containing protein
    • Taylor, J.P. et al. Aggresomes protect cells by enhancing the degradation of toxic polyglutamine-containing protein. Hum. Mol. Genet. 12, 749-757 (2003).
    • (2003) Hum. Mol. Genet , vol.12 , pp. 749-757
    • Taylor, J.P.1
  • 14
    • 0032475941 scopus 로고    scopus 로고
    • Ataxin-1 nuclear localization and aggregation: Role in polyglutamine-induced disease in SCA1 transgenic mice
    • Klement, I.A. et al. Ataxin-1 nuclear localization and aggregation: role in polyglutamine-induced disease in SCA1 transgenic mice. Cell 95, 41-53 (1998).
    • (1998) Cell , vol.95 , pp. 41-53
    • Klement, I.A.1
  • 15
    • 28644433087 scopus 로고    scopus 로고
    • Normal huntingtin function: An alternative approach to Huntington's disease
    • Cattaneo, E., Zuccato, C. & Tartari, M. Normal huntingtin function: an alternative approach to Huntington's disease. Nat. Rev. Neurosci. 6, 919-930 (2005).
    • (2005) Nat. Rev. Neurosci , vol.6 , pp. 919-930
    • Cattaneo, E.1    Zuccato, C.2    Tartari, M.3
  • 16
    • 33749042331 scopus 로고    scopus 로고
    • Transcriptional repression of PGC-1alpha by mutant huntingtin leads to mitochondrial dysfunction and neurodegeneration
    • Cui, L. et al. Transcriptional repression of PGC-1alpha by mutant huntingtin leads to mitochondrial dysfunction and neurodegeneration. Cell 127, 59-69 (2006).
    • (2006) Cell , vol.127 , pp. 59-69
    • Cui, L.1
  • 17
    • 29244462838 scopus 로고    scopus 로고
    • In vitro analysis of huntingtin-mediated transcriptional repression reveals multiple transcription factor targets
    • Zhai, W., Jeong, H., Cui, L., Krainc, D. & Tjian, R. In vitro analysis of huntingtin-mediated transcriptional repression reveals multiple transcription factor targets. Cell 123, 1241-1253 (2005).
    • (2005) Cell , vol.123 , pp. 1241-1253
    • Zhai, W.1    Jeong, H.2    Cui, L.3    Krainc, D.4    Tjian, R.5
  • 18
    • 0033757718 scopus 로고    scopus 로고
    • Inactivation of Hdh in the brain and testis results in progressive neurodegeneration and sterility in mice
    • Dragatsis, I., Levine, M.S. & Zeitlin, S. Inactivation of Hdh in the brain and testis results in progressive neurodegeneration and sterility in mice. Nat. Genet. 26, 300-306 (2000).
    • (2000) Nat. Genet , vol.26 , pp. 300-306
    • Dragatsis, I.1    Levine, M.S.2    Zeitlin, S.3
  • 19
    • 19744380273 scopus 로고    scopus 로고
    • Loss of wild-type huntingtin influences motor dysfunction and survival in the YAC128 mouse model of Huntington disease
    • Van Raamsdonk, J.M. et al. Loss of wild-type huntingtin influences motor dysfunction and survival in the YAC128 mouse model of Huntington disease. Hum. Mol. Genet. 14, 1379-1392 (2005).
    • (2005) Hum. Mol. Genet , vol.14 , pp. 1379-1392
    • Van Raamsdonk, J.M.1
  • 20
    • 0035888618 scopus 로고    scopus 로고
    • The HD mutation causes progressive lethal neurological disease in mice expressing reduced levels of huntingtin
    • Auerbach, W. et al. The HD mutation causes progressive lethal neurological disease in mice expressing reduced levels of huntingtin. Hum. Mol. Genet. 10, 2515-2523 (2001).
    • (2001) Hum. Mol. Genet , vol.10 , pp. 2515-2523
    • Auerbach, W.1
  • 21
    • 0035127907 scopus 로고    scopus 로고
    • Wild-type huntingtin reduces the cellular toxicity of mutant huntingtin in vivo
    • Leavitt, B.R. et al. Wild-type huntingtin reduces the cellular toxicity of mutant huntingtin in vivo. Am. J. Hum. Genet. 68, 313-324 (2001).
    • (2001) Am. J. Hum. Genet , vol.68 , pp. 313-324
    • Leavitt, B.R.1
  • 22
    • 0041353535 scopus 로고    scopus 로고
    • Huntingtin interacts with REST/NRSF to modulate the transcription of NRSE-controlled neuronal genes
    • Zuccato, C. et al. Huntingtin interacts with REST/NRSF to modulate the transcription of NRSE-controlled neuronal genes. Nat. Genet. 35, 76-83 (2003).
    • (2003) Nat. Genet , vol.35 , pp. 76-83
    • Zuccato, C.1
  • 23
    • 0034933959 scopus 로고    scopus 로고
    • Wild type Huntingtin reduces the cellular toxicity of mutant Huntingtin in mammalian cell models of Huntington's disease
    • Ho, L.W., Brown, R., Maxwell, M., Wyttenbach, A. & Rubinsztein, D.C. Wild type Huntingtin reduces the cellular toxicity of mutant Huntingtin in mammalian cell models of Huntington's disease. J. Med. Genet. 38, 450-452 (2001).
    • (2001) J. Med. Genet , vol.38 , pp. 450-452
    • Ho, L.W.1    Brown, R.2    Maxwell, M.3    Wyttenbach, A.4    Rubinsztein, D.C.5
  • 24
    • 33745003424 scopus 로고    scopus 로고
    • Cleavage at the caspase-6 site is required for neuronal dysfunction and degeneration due to mutant huntingtin
    • Graham, R.K. et al. Cleavage at the caspase-6 site is required for neuronal dysfunction and degeneration due to mutant huntingtin. Cell 125, 1179-1191 (2006).
    • (2006) Cell , vol.125 , pp. 1179-1191
    • Graham, R.K.1
  • 25
    • 3142636768 scopus 로고    scopus 로고
    • Huntingtin controls neurotrophic support and survival of neurons by enhancing BDNF vesicular transport along microtubules
    • Gauthier, L.R. et al. Huntingtin controls neurotrophic support and survival of neurons by enhancing BDNF vesicular transport along microtubules. Cell 118, 127-138 (2004).
    • (2004) Cell , vol.118 , pp. 127-138
    • Gauthier, L.R.1
  • 26
    • 0141844595 scopus 로고    scopus 로고
    • Beta-synuclein displays an antiapoptotic p53-dependent phenotype and protects neurons from 6-hydroxydopamine-induced caspase 3 activation: Cross-talk with alpha-synuclein and implication for Parkinson's disease
    • da Costa, C.A., Masliah, E. & Checler, F. Beta-synuclein displays an antiapoptotic p53-dependent phenotype and protects neurons from 6-hydroxydopamine-induced caspase 3 activation: cross-talk with alpha-synuclein and implication for Parkinson's disease. J. Biol. Chem. 278, 37330-37335 (2003).
    • (2003) J. Biol. Chem , vol.278 , pp. 37330-37335
    • da Costa, C.A.1    Masliah, E.2    Checler, F.3
  • 27
    • 0037421691 scopus 로고    scopus 로고
    • SCA7 knockin mice model human SCA7 and reveal gradual accumulation of mutant ataxin-7 in neurons and abnormalities in short-term plasticity
    • Yoo, S.Y. et al. SCA7 knockin mice model human SCA7 and reveal gradual accumulation of mutant ataxin-7 in neurons and abnormalities in short-term plasticity. Neuron 37, 383-401 (2003).
    • (2003) Neuron , vol.37 , pp. 383-401
    • Yoo, S.Y.1
  • 28
    • 0037726598 scopus 로고    scopus 로고
    • Interaction of Akt-phosphorylated ataxin-1 with 14-3-3 mediates neurodegeneration in spinocerebellar ataxia type 1
    • Chen, H.K. et al. Interaction of Akt-phosphorylated ataxin-1 with 14-3-3 mediates neurodegeneration in spinocerebellar ataxia type 1. Cell 113, 457-468 (2003).
    • (2003) Cell , vol.113 , pp. 457-468
    • Chen, H.K.1
  • 29
    • 0032530393 scopus 로고    scopus 로고
    • Complex formation by the Drosophila MSL proteins: Role of the MSL2 RING finger in protein complex assembly
    • Copps, K. et al. Complex formation by the Drosophila MSL proteins: role of the MSL2 RING finger in protein complex assembly. EMBO J. 17, 5409-5417 (1998).
    • (1998) EMBO J , vol.17 , pp. 5409-5417
    • Copps, K.1


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