메뉴 건너뛰기




Volumn 4, Issue MAY, 2015, Pages 1-46

A native interactor scaffolds and stabilizes toxic Ataxin-1 oligomers in SCA1

Author keywords

[No Author keywords available]

Indexed keywords

ATAXIN 1; CAPICUA; TRANSCRIPTION FACTOR; UNCLASSIFIED DRUG; ATXN1 PROTEIN, MOUSE; CIC PROTEIN, MOUSE; PEPTIDE; POLYGLUTAMINE; REPRESSOR PROTEIN;

EID: 84930648934     PISSN: None     EISSN: 2050084X     Source Type: Journal    
DOI: 10.7554/eLife.07558     Document Type: Article
Times cited : (26)

References (44)
  • 1
    • 84858978818 scopus 로고    scopus 로고
    • Protein misfolded oligomers: Experimental approaches, mechanism of formation, and structure-toxicity relationships
    • Bemporad, F., and Chiti, F. (2012). Protein misfolded oligomers: experimental approaches, mechanism of formation, and structure-toxicity relationships. Chemistry & biology 19, 315-327.
    • (2012) Chemistry & biology , vol.19 , pp. 315-327
    • Bemporad, F.1    Chiti, F.2
  • 2
    • 84857642949 scopus 로고    scopus 로고
    • The toxic Abeta oligomer and Alzheimer's disease: An emperor in need of clothes
    • Benilova, I., Karran, E., and De Strooper, B. (2012). The toxic Abeta oligomer and Alzheimer's disease: an emperor in need of clothes. Nature neuroscience 15, 349-357.
    • (2012) Nature neuroscience , vol.15 , pp. 349-357
    • Benilova, I.1    Karran, E.2    De Strooper, B.3
  • 5
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • Chiti, F., and Dobson, C.M. (2006). Protein misfolding, functional amyloid, and human disease. Annual review of biochemistry 75, 333-366.
    • (2006) Annual review of biochemistry , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.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. Nature genetics 19, 148-154.
    • (1998) Nature genetics , 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
    • 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., Ciechanover, 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    Ciechanover, A.6    Orr, H.T.7    Beaudet, A.L.8    Zoghbi, H.Y.9
  • 9
    • 28444444502 scopus 로고    scopus 로고
    • Polyglutamine is not all: The functional role of the AXH domain in the ataxin-1 protein
    • de Chiara, C., Menon, R.P., Dal Piaz, F., Calder, L., and Pastore, A. (2005). Polyglutamine is not all: the functional role of the AXH domain in the ataxin-1 protein. Journal of molecular biology 354, 883-893.
    • (2005) Journal of molecular biology , vol.354 , pp. 883-893
    • de Chiara, C.1    Menon, R.P.2    Dal Piaz, F.3    Calder, L.4    Pastore, A.5
  • 10
  • 12
    • 57649148788 scopus 로고    scopus 로고
    • Structural classification of toxic amyloid oligomers
    • Glabe, C.G. (2008). Structural classification of toxic amyloid oligomers. The Journal of biological chemistry 283, 29639-29643.
    • (2008) The Journal of biological chemistry , vol.283 , pp. 29639-29643
    • Glabe, C.G.1
  • 13
    • 33644861975 scopus 로고    scopus 로고
    • Common structure and toxic function of amyloid oligomers implies a common mechanism of pathogenesis
    • Glabe, C.G., and Kayed, R. (2006). Common structure and toxic function of amyloid oligomers implies a common mechanism of pathogenesis. Neurology 66, S74-78.
    • (2006) Neurology , vol.66 , pp. S74-S78
    • Glabe, C.G.1    Kayed, R.2
  • 14
    • 0021207461 scopus 로고
    • Alzheimer's disease and Down's syndrome: Sharing of a unique cerebrovascular amyloid fibril protein
    • Glenner, G.G., and Wong, C.W. (1984). Alzheimer's disease and Down's syndrome: sharing of a unique cerebrovascular amyloid fibril protein. Biochemical and biophysical research communications 122, 1131- 1135.
    • (1984) Biochemical and biophysical research communications , vol.122 , pp. 1131-1135
    • Glenner, G.G.1    Wong, C.W.2
  • 17
    • 84897954120 scopus 로고    scopus 로고
    • Therapeutic approaches ches against common structural features of toxic oligomers shared by multiple amyloidogenic proteins
    • Guerrero-Munoz, M.J., Castillo-Carranza, D.L., and Kayed, R. (2014a). Therapeutic approaches ches against common structural features of toxic oligomers shared by multiple amyloidogenic proteins. Biochemical pharmacology 88, 468-478.
    • (2014) Biochemical pharmacology , vol.88 , pp. 468-478
    • Guerrero-Munoz, M.J.1    Castillo-Carranza, D.L.2    Kayed, R.3
  • 21
    • 36749078121 scopus 로고    scopus 로고
    • Fibril specific, conformation dependent antibodies recognize a generic epitope common to amyloid fibrils and fibrillar oligomers that is absent in prefibrillar oligomers
    • Kayed, R., Head, E., Sarsoza, F., Saing, T., Cotman, C.W., Necula, M., Margol, L., Wu, J., Breydo, L., Thompson, J.L., et al. (2007). Fibril specific, conformation dependent antibodies recognize a generic epitope common to amyloid fibrils and fibrillar oligomers that is absent in prefibrillar oligomers. Molecular neurodegeneration 2, 18.
    • (2007) Molecular neurodegeneration , vol.2 , pp. 18
    • Kayed, R.1    Head, E.2    Sarsoza, F.3    Saing, T.4    Cotman, C.W.5    Necula, M.6    Margol, L.7    Wu, J.8    Breydo, L.9    Thompson, J.L.10
  • 22
    • 0242668337 scopus 로고    scopus 로고
    • Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
    • Kayed, R., Head, E., Thompson, J.L., McIntire, T.M., Milton, S.C., Cotman, C.W., and Glabe, C.G. (2003). Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis. Science 300, 486-489.
    • (2003) Science , vol.300 , pp. 486-489
    • Kayed, R.1    Head, E.2    Thompson, J.L.3    McIntire, T.M.4    Milton, S.C.5    Cotman, C.W.6    Glabe, C.G.7
  • 23
    • 84875324689 scopus 로고    scopus 로고
    • Structural basis of protein complex formation and reconfiguration by polyglutamine disease protein Ataxin-1 and Capicua
    • Kim, E., Lu, H.C., Zoghbi, H.Y., and Song, J.J. (2013). Structural basis of protein complex formation and reconfiguration by polyglutamine disease protein Ataxin-1 and Capicua. Genes & development 27, 590- 595.
    • (2013) Genes & development , vol.27 , pp. 590-595
    • Kim, E.1    Lu, H.C.2    Zoghbi, H.Y.3    Song, J.J.4
  • 29
    • 84871414210 scopus 로고    scopus 로고
    • The many faces of alpha-synuclein: From structure and toxicity to therapeutic target
    • Lashuel, H.A., Overk, C.R., Oueslati, A., and Masliah, E. (2013). The many faces of alpha-synuclein: from structure and toxicity to therapeutic target. Nature reviews Neuroscience 14, 38-48.
    • (2013) Nature reviews Neuroscience , vol.14 , pp. 38-48
    • Lashuel, H.A.1    Overk, C.R.2    Oueslati, A.3    Masliah, E.4
  • 33
    • 33646687963 scopus 로고    scopus 로고
    • A protein-protein interaction network for human inherited ataxias and disorders of Purkinje cell degeneration
    • Lim, J., Hao, T., Shaw, C., Patel, A.J., Szabo, G., Rual, J.F., Fisk, C.J., Li, N., Smolyar, A., Hill, D..E., et al. (2006). A protein-protein interaction network for human inherited ataxias and disorders of Purkinje cell degeneration. Cell 125, 801-814.
    • (2006) Cell , vol.125 , pp. 801-814
    • Lim, J.1    Hao, T.2    Shaw, C.3    Patel, A.J.4    Szabo, G.5    Rual, J.F.6    Fisk, C.J.7    Li, N.8    Smolyar, A.9    Hill, D.E.10
  • 34
    • 0034701278 scopus 로고    scopus 로고
    • Repeat instability and motor incoordination in mice with a targeted expanded CAG repeat in the Sca1 locus
    • Lorenzetti, D., Watase, K., Xu, B., Matzuk, M.M., Orr, H.T., and Zoghbi, H.Y. (2000). Repeat instability and motor incoordination in mice with a targeted expanded CAG repeat in the Sca1 locus. Human molecular genetics 9, 779-785.
    • (2000) Human molecular genetics , vol.9 , pp. 779-785
    • Lorenzetti, D.1    Watase, K.2    Xu, B.3    Matzuk, M.M.4    Orr, H.T.5    Zoghbi, H.Y.6
  • 36
    • 84885470591 scopus 로고    scopus 로고
    • Transfer of human alpha-synuclein from the olfactory bulb to interconnected brain regions in mice
    • Rey, N.L., Petit, G.H., Bousset, L., Melki, R., and Brundin, P. (2013). Transfer of human alpha-synuclein from the olfactory bulb to interconnected brain regions in mice. Acta neuropathologica 126, 555-573.
    • (2013) Acta neuropathologica , vol.126 , pp. 555-573
    • Rey, N.L.1    Petit, G.H.2    Bousset, L.3    Melki, R.4    Brundin, P.5
  • 37
    • 70349199064 scopus 로고    scopus 로고
    • Multi-domain misfolding: Understanding the aggregation pathway of polyglutamine proteins
    • Saunders, H.M., and Bottomley, S.P. (2009). Multi-domain misfolding: understanding the aggregation pathway of polyglutamine proteins. Protein engineering, design & selection: PEDS 22, 447-451.
    • (2009) Protein engineering, design & selection: PEDS , vol.22 , pp. 447-451
    • Saunders, H.M.1    Bottomley, S.P.2
  • 40
    • 0028882424 scopus 로고
    • Prion propagation in mice expressing human and chimeric PrP transgenes implicates the interaction of cellular PrP with another protein
    • Telling, G.C., Scott, M., Mastrianni, J., Gabizon, R., Torchia, M., Cohen, F.E., DeArmond, S.J., and Prusiner, S.B. (1995). Prion propagation in mice expressing human and chimeric PrP transgenes implicates the interaction of cellular PrP with another protein. Cell 83, 79-90.
    • (1995) Cell , vol.83 , pp. 79-90
    • Telling, G.C.1    Scott, M.2    Mastrianni, J.3    Gabizon, R.4    Torchia, M.5    Cohen, F.E.6    DeArmond, S.J.7    Prusiner, S.B.8
  • 42
    • 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., 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 Sca1 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
  • 43
  • 44
    • 65549134765 scopus 로고    scopus 로고
    • Pathogenic mechanisms of a polyglutamine-mediated neurodegenerative disease, spinocerebellar ataxia type 1
    • Zoghbi, H.Y., and Orr, H.T. (2009). Pathogenic mechanisms of a polyglutamine-mediated neurodegenerative disease, spinocerebellar ataxia type 1. The Journal of biological chemistry 284, 7425- 7429.
    • (2009) The Journal of biological chemistry , vol.284 , pp. 7425-7429
    • Zoghbi, H.Y.1    Orr, H.T.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.