메뉴 건너뛰기




Volumn 18, Issue 24, 2009, Pages 4843-4852

Preventing Ataxin-3 protein cleavage mitigates degeneration in a Drosophila model of SCA3

Author keywords

[No Author keywords available]

Indexed keywords

ATAXIN 3; CASPASE;

EID: 70450191208     PISSN: 09646906     EISSN: 14602083     Source Type: Journal    
DOI: 10.1093/hmg/ddp456     Document Type: Article
Times cited : (53)

References (27)
  • 1
    • 40349085851 scopus 로고    scopus 로고
    • Gamma-secretase modulation and its promise for Alzheimer's disease: A rationale for drug discovery
    • Beher, D. (2008) Gamma-secretase modulation and its promise for Alzheimer's disease: A rationale for drug discovery. Curr. Top. Med. Chem., 8, 34-37.
    • (2008) Curr. Top. Med. Chem , vol.8 , pp. 34-37
    • Beher, D.1
  • 2
    • 67149144477 scopus 로고    scopus 로고
    • Caspases as therapeutic targets in Alzheimer's disease: Is it time to 'cut' to the chase?
    • Rohn, T.T. and Head, E. (2009) Caspases as therapeutic targets in Alzheimer's disease: Is it time to 'cut' to the chase? Int. J. Clin. Exp. Pathol., 2, 108-118.
    • (2009) Int. J. Clin. Exp. Pathol , vol.2 , pp. 108-118
    • Rohn, T.T.1    Head, E.2
  • 5
    • 25644434918 scopus 로고    scopus 로고
    • Purification of neuronal inclusions of patients with Huntington's disease reveals a broad range of N-terminal fragments of expanded huntingtin and insoluble polymers
    • Hoffner, G., Island, M.L. and Djian, P. (2005) Purification of neuronal inclusions of patients with Huntington's disease reveals a broad range of N-terminal fragments of expanded huntingtin and insoluble polymers. J. Neurochem., 95, 125-136.
    • (2005) J. Neurochem , vol.95 , pp. 125-136
    • Hoffner, G.1    Island, M.L.2    Djian, P.3
  • 6
    • 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., Deng, Y., Slow, E.J., Haigh, B., Bissada, N., Lu, G., Pearson, J., Shehadeh, J., Bertram, L., Murphy, Z. et al. (2006) Cleavage at the caspase-6 site is required for neuronal dysfunction and degeneration due to mutant huntingtin. Cell, 125, 1179-1191.
    • (2006) Cell , vol.125 , pp. 1179-1191
    • Graham, R.K.1    Deng, Y.2    Slow, E.J.3    Haigh, B.4    Bissada, N.5    Lu, G.6    Pearson, J.7    Shehadeh, J.8    Bertram, L.9    Murphy, Z.10
  • 7
    • 20844462057 scopus 로고    scopus 로고
    • A mutant ataxin-3 putative-cleavage fragment in brains of Machado-Joseph disease patients and transgenic mice is cytotoxic above a critical concentration
    • Goti, D., Katzen, S.M., Mez, J., Kurtis, N., Kiluk, J., Ben-Haiem, L., Jenkins, N.A., Copeland, N.G., Kakizuka, A., Sharp, A.H. et al. (2004) A mutant ataxin-3 putative-cleavage fragment in brains of Machado-Joseph disease patients and transgenic mice is cytotoxic above a critical concentration. J. Neurosci., 24, 10266-10279.
    • (2004) J. Neurosci , vol.24 , pp. 10266-10279
    • Goti, D.1    Katzen, S.M.2    Mez, J.3    Kurtis, N.4    Kiluk, J.5    Ben-Haiem, L.6    Jenkins, N.A.7    Copeland, N.G.8    Kakizuka, A.9    Sharp, A.H.10
  • 9
    • 2542445545 scopus 로고    scopus 로고
    • Caspase-mediated proteolysis of the polyglutamine disease protein ataxin-3
    • Berke, S.J., Schmied, F.A., Brunt, E.R., Ellerby, L.M. and Paulson, H.L. (2004) Caspase-mediated proteolysis of the polyglutamine disease protein ataxin-3. J. Neurochem., 89, 908-918.
    • (2004) J. Neurochem , vol.89 , pp. 908-918
    • Berke, S.J.1    Schmied, F.A.2    Brunt, E.R.3    Ellerby, L.M.4    Paulson, H.L.5
  • 10
    • 34147136044 scopus 로고    scopus 로고
    • CREB-binding protein modulates repeat instability in a Drosophila model for polyQ disease
    • Jung, J. and Bonini, N. (2007) CREB-binding protein modulates repeat instability in a Drosophila model for polyQ disease. Science 315, 1857-1859.
    • (2007) Science , vol.315 , pp. 1857-1859
    • Jung, J.1    Bonini, N.2
  • 11
    • 40149101562 scopus 로고    scopus 로고
    • Polyglutamine genes interact to modulate the severity and progression of neurodegeneration in Drosophila
    • Lessing, D. and Bonini, N.M. (2008) Polyglutamine genes interact to modulate the severity and progression of neurodegeneration in Drosophila. PLoS Biol., 6, 266-274.
    • (2008) PLoS Biol , vol.6 , pp. 266-274
    • Lessing, D.1    Bonini, N.M.2
  • 12
    • 45749147456 scopus 로고    scopus 로고
    • RNA toxicity is a component of ataxin-3 degeneration in Drosophila
    • Li, L.B., Yu, Z., Teng, X. and Bonini, N.M. (2008) RNA toxicity is a component of ataxin-3 degeneration in Drosophila. Nature, 453 1107-1011.
    • (2008) Nature , vol.453 , pp. 1107-1011
    • Li, L.B.1    Yu, Z.2    Teng, X.3    Bonini, N.M.4
  • 14
    • 0345099501 scopus 로고    scopus 로고
    • The polyglutamine neurodegenerative protein ataxin-3 binds polyubiquitylated proteins and has ubiquitin protease activity
    • Burnett, B., Li, F. and Pittman, R.N. (2003) The polyglutamine neurodegenerative protein ataxin-3 binds polyubiquitylated proteins and has ubiquitin protease activity. Hum. Mol. Genet., 12, 3195-3205.
    • (2003) Hum. Mol. Genet , vol.12 , pp. 3195-3205
    • Burnett, B.1    Li, F.2    Pittman, R.N.3
  • 15
    • 15444372240 scopus 로고    scopus 로고
    • The polyglutamine neurodegenerative protein ataxin 3 regulates aggresome formation
    • Burnett, B.G. and Pittman, R.N. (2005) The polyglutamine neurodegenerative protein ataxin 3 regulates aggresome formation. Proc. Natl Acad. Sci. USA, 102, 4330-4335.
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 4330-4335
    • Burnett, B.G.1    Pittman, R.N.2
  • 16
    • 55549086868 scopus 로고    scopus 로고
    • The deubiquitinating enzyme ataxin-3, a polyglutamine disease protein, edits Lys63 linkages in mixed linkage ubiquitin chains
    • Winborn, B.J., Travis, S.M., Todi, S.V., Scaglione, K.M., Xu, P., Williams, A.J., Cohen, R.E., Peng, J. and Paulson, H.L. (2008) The deubiquitinating enzyme ataxin-3, a polyglutamine disease protein, edits Lys63 linkages in mixed linkage ubiquitin chains. J. Biol. Chem., 283, 26436-26443.
    • (2008) J. Biol. Chem , vol.283 , pp. 26436-26443
    • Winborn, B.J.1    Travis, S.M.2    Todi, S.V.3    Scaglione, K.M.4    Xu, P.5    Williams, A.J.6    Cohen, R.E.7    Peng, J.8    Paulson, H.L.9
  • 18
    • 34547129609 scopus 로고    scopus 로고
    • Calpain inhibition is sufficient to suppress aggregation of polyglutamine-expanded ataxin-3
    • Haacke, A., Hartl, F.U. and Breuer, P. (2007) Calpain inhibition is sufficient to suppress aggregation of polyglutamine-expanded ataxin-3. J. Biol. Chem., 282, 18851-18856.
    • (2007) J. Biol. Chem , vol.282 , pp. 18851-18856
    • Haacke, A.1    Hartl, F.U.2    Breuer, P.3
  • 20
    • 0036798685 scopus 로고    scopus 로고
    • Intranuclear ataxin1 inclusions contain both fast- and slow-exchanging components
    • Stenoien, D.L., Mielke, M. and Mancini, M.A. (2002) Intranuclear ataxin1 inclusions contain both fast- and slow-exchanging components. Nat. Cell Biol., 4, 806-810.
    • (2002) Nat. Cell Biol , vol.4 , pp. 806-810
    • Stenoien, D.L.1    Mielke, M.2    Mancini, M.A.3
  • 22
    • 33745256182 scopus 로고    scopus 로고
    • Small N-terminal mutant huntingtin fragments, but not wild type, are mainly present in monomeric form: Implications for pathogenesis
    • Cong, S.Y., Pepers, B.A., Roos, R.A., van Ommen, G.J. and Dorsman, J.C. (2006) Small N-terminal mutant huntingtin fragments, but not wild type, are mainly present in monomeric form: Implications for pathogenesis. Exp. Neurol., 199, 257-264.
    • (2006) Exp. Neurol , vol.199 , pp. 257-264
    • Cong, S.Y.1    Pepers, B.A.2    Roos, R.A.3    van Ommen, G.J.4    Dorsman, J.C.5
  • 24
    • 0034990512 scopus 로고    scopus 로고
    • Tissue transglutaminase selectively modifies proteins associated with truncated mutant huntingtin in intact cells
    • Chun, W., Lesort, M., Tucholski, J., Faber, P.W., MacDonald, M.E., Ross, C.A. and Johnson, G.V. (2001) Tissue transglutaminase selectively modifies proteins associated with truncated mutant huntingtin in intact cells. Neurobiol. Dis., 8, 391-404.
    • (2001) Neurobiol. Dis , vol.8 , pp. 391-404
    • Chun, W.1    Lesort, M.2    Tucholski, J.3    Faber, P.W.4    MacDonald, M.E.5    Ross, C.A.6    Johnson, G.V.7
  • 25
    • 0035940412 scopus 로고    scopus 로고
    • Caspase 3-cleaved N-terminal fragments of wild-type and mutant huntingtin are present in normal and Huntington's disease brains, associate with membranes, and undergo calpain-dependent proteolysis
    • Kim, Y.J., Yi, Y., Sapp, E., Wang, Y., Cuiffo, B., Kegel, K.B., Qin, Z.H., Aronin, N. and DiFiglia, M. (2001) Caspase 3-cleaved N-terminal fragments of wild-type and mutant huntingtin are present in normal and Huntington's disease brains, associate with membranes, and undergo calpain-dependent proteolysis. Proc. Natl Acad. Sci. USA, 98 12784-12789.
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 12784-12789
    • Kim, Y.J.1    Yi, Y.2    Sapp, E.3    Wang, Y.4    Cuiffo, B.5    Kegel, K.B.6    Qin, Z.H.7    Aronin, N.8    DiFiglia, M.9
  • 26
    • 38049151005 scopus 로고    scopus 로고
    • Suppression of polyglutamine toxicity by the yeast Sup35 prion domain in Drosophila
    • Li, L.B., Xu, K. and Bonini, N.M. (2007) Suppression of polyglutamine toxicity by the yeast Sup35 prion domain in Drosophila. J. Biol. Chem., 282, 37694-37701.
    • (2007) J. Biol. Chem , vol.282 , pp. 37694-37701
    • Li, L.B.1    Xu, K.2    Bonini, N.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.