메뉴 건너뛰기




Volumn 288, Issue 48, 2013, Pages 34460-34469

Ubiquitination regulates the neuroprotective function of the deubiquitinase ataxin-3 in vivo

Author keywords

[No Author keywords available]

Indexed keywords

C TERMINUS; CELLULAR PROCESS; DROSOPHILA MELANOGASTER; LYSINE RESIDUES; PROTEASE ACTIVITIES; TOXIC PROTEINS; UBIQUITIN LIGASES; UBIQUITINATION;

EID: 84889049439     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.513903     Document Type: Article
Times cited : (48)

References (43)
  • 1
    • 79959906646 scopus 로고    scopus 로고
    • Balancing act deubiquitinating enzymes in the nervous system
    • Todi, S. V., and Paulson, H. L. (2011) Balancing act: deubiquitinating enzymes in the nervous system. Trends Neurosci. 34, 370-382
    • (2011) Trends Neurosci , vol.34 , pp. 370-382
    • Todi, S.V.1    Paulson, H.L.2
  • 2
    • 84858119736 scopus 로고    scopus 로고
    • Cellular functions of the DUBs
    • Clague, M. J., Coulson, J. M., and Urbé, S. (2012) Cellular functions of the DUBs. J. Cell Sci. 125, 277-286
    • (2012) J. Cell Sci , vol.125 , pp. 277-286
    • Clague, M.J.1    Coulson, J.M.2    Urbé, S.3
  • 4
    • 77949733627 scopus 로고    scopus 로고
    • Emerging roles of deubiquitinases in cancer-associated pathways
    • Sacco, J. J., Coulson, J. M., Clague, M. J., and Urbé, S. (2010) Emerging roles of deubiquitinases in cancer-associated pathways. IUBMB Life 62, 140-157
    • (2010) IUBMB Life , vol.62 , pp. 140-157
    • Sacco, J.J.1    Coulson, J.M.2    Clague, M.J.3    Urbé, S.4
  • 7
    • 84940331098 scopus 로고    scopus 로고
    • Should deubiquitinating enzymes be targeted for therapy?
    • Todi, S., and Das, C. (2012) Should deubiquitinating enzymes be targeted for therapy? Clin. Pharmacol. Biopharmaceutics 1, 1000e108
    • (2012) Clin Pharmacol. Biopharmaceutics , vol.1
    • Todi, S.1    Das, C.2
  • 9
    • 79955941973 scopus 로고    scopus 로고
    • PTMs in conversation: Activity and function of deubiquitinating enzymes regulated via post-translational modifications
    • Kessler, B. M., and Edelmann, M. J. (2011) PTMs in conversation: activity and function of deubiquitinating enzymes regulated via post-translational modifications. Cell Biochem. Biophys. 60, 21-38
    • (2011) Cell Biochem. Biophys , vol.60 , pp. 21-38
    • Kessler, B.M.1    Edelmann, M.J.2
  • 10
    • 84879037295 scopus 로고    scopus 로고
    • JosD1 a membrane-targeted deubiquitinating enzyme is activated by ubiquitination and regulates membrane dynamics cell motility and endocytosis
    • Seki, T., Gong, L., Williams, A. J., Sakai, N., Todi, S. V., and Paulson, H. L. (2013) JosD1, a membrane-targeted deubiquitinating enzyme, is activated by ubiquitination and regulates membrane dynamics, cell motility and endocytosis. J. Biol. Chem. 288, 17145-17155
    • (2013) J Biol Chem , vol.288 , pp. 17145-17155
    • Seki, T.1    Gong, L.2    Williams, A.J.3    Sakai, N.4    Todi, S.V.5    Paulson, H.L.6
  • 11
    • 60549100850 scopus 로고    scopus 로고
    • Ubiquitination directly enhances activity of the deubiquitinating enzyme ataxin-3
    • Todi, S. V., Winborn, B. J., Scaglione, K. M., Blount, J. R., Travis, S. M., and Paulson, H. L. (2009) Ubiquitination directly enhances activity of the deubiquitinating enzyme ataxin-3. EMBO J. 28, 372-382
    • (2009) EMBO J. , vol.28 , pp. 372-382
    • Todi, S.V.1    Winborn, B.J.2    Scaglione, K.M.3    Blount, J.R.4    Travis, S.M.5    Paulson, H.L.6
  • 12
    • 67649634849 scopus 로고    scopus 로고
    • Defining the human deubiquitinating enzyme interaction landscape
    • Sowa, M. E., Bennett, E. J., Gygi, S. P., and Harper, J. W. (2009) Defining the human deubiquitinating enzyme interaction landscape. Cell 138, 389-403
    • (2009) Cell , vol.138 , pp. 389-403
    • Sowa, M.E.1    Bennett, E.J.2    Gygi, S.P.3    Harper, J.W.4
  • 13
    • 78649811312 scopus 로고    scopus 로고
    • Activity and cellular functions of the deubiquitinating enzyme and polyglutamine disease protein ataxin-3 are regulated by ubiquitination at lysine 117
    • Todi, S. V., Scaglione, K. M., Blount, J. R., Basrur, V., Conlon, K. P., Pastore, A., Elenitoba-Johnson, K., and Paulson, H. L. (2010) Activity and cellular functions of the deubiquitinating enzyme and polyglutamine disease protein ataxin-3 are regulated by ubiquitination at lysine 117. J. Biol. Chem. 285, 39303-39313
    • (2010) J Biol Chem , vol.285 , pp. 39303-39313
    • Todi, S.V.1    Scaglione, K.M.2    Blount, J.R.3    Basrur, V.4    Conlon, K.P.5    Pastore, A.6    Elenitoba-Johnson, K.7    Paulson, H.L.8
  • 14
    • 34249845272 scopus 로고    scopus 로고
    • Reversible monoubiquitination regulates the Parkinson disease-associated ubiquitin hydrolase UCHL1
    • Meray, R. K., and Lansbury, P. T., Jr. (2007) Reversible monoubiquitination regulates the Parkinson disease-associated ubiquitin hydrolase UCHL1. J. Biol. Chem. 282, 10567-10575
    • (2007) J. Biol. Chem , vol.282 , pp. 10567-10575
    • Meray, R.K.1    Lansbury Jr., P.T.2
  • 15
    • 68149163523 scopus 로고    scopus 로고
    • The UBA-UIM domains of the USP25 regulate the enzyme ubiquitination state and modulate substrate recognition
    • Denuc, A., Bosch-Comas, A., Gonzàlez-Duarte, R., and Marfany, G. (2009) The UBA-UIM domains of the USP25 regulate the enzyme ubiquitination state and modulate substrate recognition. PLoS One 4, e5571
    • (2009) PLoS One , vol.4
    • Denuc, A.1    Bosch-Comas, A.2    Gonzàlez-Duarte, R.3    Marfany, G.4
  • 16
    • 84860660444 scopus 로고    scopus 로고
    • Toward understanding Machado-Joseph disease
    • Costa Mdo, C., and Paulson, H. L. (2012) Toward understanding Machado-Joseph disease. Prog. Neurobiol. 97, 239-257
    • (2012) Prog Neurobiol , vol.97 , pp. 239-257
    • Costa Mdo, C.1    Paulson, H.L.2
  • 17
  • 18
    • 52049086030 scopus 로고    scopus 로고
    • (Waxman, S. G., ed) 1st Ed., Academic Press, London
    • Todi, S. V., Williams, A., and Paulson, H. (2007) in Molecular Neurology (Waxman, S. G., ed) 1st Ed., pp. 257-276, Academic Press, London
    • (2007) Molecular Neurology , pp. 257-276
    • Todi, S.V.1    Williams, A.2    Paulson, H.3
  • 19
    • 52049093169 scopus 로고    scopus 로고
    • Polyglutamine neurodegeneration: Protein misfolding revisited
    • Williams, A. J., and Paulson, H. L. (2008) Polyglutamine neurodegeneration: protein misfolding revisited. Trends Neurosci. 31, 521-528
    • (2008) Trends Neurosci , vol.31 , pp. 521-528
    • Williams, A.J.1    Paulson, H.L.2
  • 21
    • 55549086868 scopus 로고    scopus 로고
    • The deubiquitinating enzyme ataxin-3, a polyglutamine disease protein, edits Lys-63 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 Lys-63 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
  • 22
    • 35748947239 scopus 로고    scopus 로고
    • Cellular turnover of the polyglutamine disease protein ataxin-3 is regulated by its catalytic activity
    • Todi, S. V., Laco, M. N., Winborn, B. J., Travis, S. M., Wen, H. M., and Paulson, H. L. (2007) Cellular turnover of the polyglutamine disease protein ataxin-3 is regulated by its catalytic activity. J. Biol. Chem. 282, 29348-29358
    • (2007) J. Biol. Chem , vol.282 , pp. 29348-29358
    • Todi, S.V.1    Laco, M.N.2    Winborn, B.J.3    Travis, S.M.4    Wen, H.M.5    Paulson, H.L.6
  • 23
    • 84860750274 scopus 로고    scopus 로고
    • Ubiquitin-specific protease 25 functions in endoplasmic reticulum-associated degradation
    • Blount, J. R., Burr, A. A., Denuc, A., Marfany, G., and Todi, S. V. (2012) Ubiquitin-specific protease 25 functions in endoplasmic reticulum-associated degradation. PLoS One 7, e36542
    • (2012) PLoS One , vol.7
    • Blount, J.R.1    Burr, A.A.2    Denuc, A.3    Marfany, G.4    Todi, S.V.5
  • 24
    • 18944408058 scopus 로고    scopus 로고
    • Myosin VIIA defects, which underlie the Usher 1B syndrome in humans, lead to deafness in Drosophila
    • Todi, S. V., Franke, J. D., Kiehart, D. P., and Eberl, D. F. (2005) Myosin VIIA defects, which underlie the Usher 1B syndrome in humans, lead to deafness in Drosophila. Curr. Biol. 15, 862-868
    • (2005) Curr. Biol , vol.15 , pp. 862-868
    • Todi, S.V.1    Franke, J.D.2    Kiehart, D.P.3    Eberl, D.F.4
  • 25
    • 47749118401 scopus 로고    scopus 로고
    • Myosin VIIA, important for human auditory function, is necessary for Drosophila auditory organ development
    • Todi, S. V., Sivan-Loukianova, E., Jacobs, J. S., Kiehart, D. P., and Eberl, D. F. (2008) Myosin VIIA, important for human auditory function, is necessary for Drosophila auditory organ development. PLoS One 3, e2115
    • (2008) PLoS One , vol.3
    • Todi, S.V.1    Sivan-Loukianova, E.2    Jacobs, J.S.3    Kiehart, D.P.4    Eberl, D.F.5
  • 27
    • 0027160708 scopus 로고
    • Targeted gene expression as a means of altering cell fates and generating dominant phenotypes
    • Brand, A. H., and Perrimon, N. (1993) Targeted gene expression as a means of altering cell fates and generating dominant phenotypes. Development 118, 401-415
    • (1993) Development , vol.118 , pp. 401-415
    • Brand, A.H.1    Perrimon, N.2
  • 28
    • 18544392423 scopus 로고    scopus 로고
    • Expanded polyglutamine protein forms nuclear inclusions and causes neural degeneration in Drosophila
    • Warrick, J. M., Paulson, H. L., Gray-Board, G. L., Bui, Q. T., Fischbeck, K. H., Pittman, R. N., and Bonini, N. M. (1998) Expanded polyglutamine protein forms nuclear inclusions and causes neural degeneration in Drosophila. Cell 93, 939-949
    • (1998) Cell , vol.93 , pp. 939-949
    • Warrick, J.M.1    Paulson, H.L.2    Gray-Board, G.L.3    Bui, Q.T.4    Fischbeck, K.H.5    Pittman, R.N.6    Bonini, N.M.7
  • 29
    • 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
  • 31
    • 25844487226 scopus 로고    scopus 로고
    • Diseases of unstable repeat expansion: Mechanisms and common principles
    • Gatchel, J. R., and Zoghbi, H. Y. (2005) Diseases of unstable repeat expansion: mechanisms and common principles. Nat. Rev. Genet. 6, 743-755
    • (2005) Nat. Rev. Genet , vol.6 , pp. 743-755
    • Gatchel, J.R.1    Zoghbi, H.Y.2
  • 32
    • 37549004790 scopus 로고    scopus 로고
    • Suppression of neurodegeneration and increased neurotransmission caused by expanded full-length huntingtin accumulating in the cytoplasm
    • Romero, E., Cha, G. H., Verstreken, P., Ly, C. V., Hughes, R. E., Bellen, H. J., and Botas, J. (2008) Suppression of neurodegeneration and increased neurotransmission caused by expanded full-length huntingtin accumulating in the cytoplasm. Neuron 57, 27-40
    • (2008) Neuron , vol.57 , pp. 27-40
    • Romero, E.1    Cha, G.H.2    Verstreken, P.3    Ly, C.V.4    Hughes, R.E.5    Bellen, H.J.6    Botas, J.7
  • 33
    • 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
  • 34
    • 83455162742 scopus 로고    scopus 로고
    • Protein interacting with C kinase (PICK1) is a suppressor of spinocerebellar ataxia 3-associated neurodegeneration in Drosophila
    • McGurk, L., and Bonini, N. M. (2012) Protein interacting with C kinase (PICK1) is a suppressor of spinocerebellar ataxia 3-associated neurodegeneration in Drosophila. Hum. Mol. Genet. 21, 76-84
    • (2012) Hum Mol Genet , vol.21 , pp. 76-84
    • McGurk, L.1    Bonini, N.M.2
  • 36
    • 33845874433 scopus 로고    scopus 로고
    • Brain CHIP: Removing the culprits in neurodegenerative disease
    • Dickey, C. A., Patterson, C., Dickson, D., and Petrucelli, L. (2007) Brain CHIP: removing the culprits in neurodegenerative disease. Trends Mol. Med. 13, 32-38
    • (2007) Trends Mol. Med , vol.13 , pp. 32-38
    • Dickey, C.A.1    Patterson, C.2    Dickson, D.3    Petrucelli, L.4
  • 37
    • 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. U.S.A. 102, 4330-4335
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 4330-4335
    • Burnett, B.G.1    Pittman, R.N.2
  • 38
    • 77949450752 scopus 로고    scopus 로고
    • Proteotoxic stress increases nuclear localization of ataxin-3
    • Reina, C. P., Zhong, X., and Pittman, R. N. (2010) Proteotoxic stress increases nuclear localization of ataxin-3. Hum. Mol. Genet. 19, 235-249
    • (2010) Hum. Mol. Genet , vol.19 , pp. 235-249
    • Reina, C.P.1    Zhong, X.2    Pittman, R.N.3
  • 42
    • 77549088508 scopus 로고    scopus 로고
    • Polyglutamine-induced neurodegeneration in SCA3 is not mitigated by non-expanded ataxin-3: Conclusions from double-transgenic mouse models
    • Hübener, J., and Riess, O. (2010) Polyglutamine-induced neurodegeneration in SCA3 is not mitigated by non-expanded ataxin-3: conclusions from double-transgenic mouse models. Neurobiol. Dis. 38, 116-124
    • (2010) Neurobiol. Dis , vol.38 , pp. 116-124
    • Hübener, J.1    Riess, O.2
  • 43
    • 29044448970 scopus 로고    scopus 로고
    • Nonmuscle myosin II generates forces that transmit tension and drive contraction in multiple tissues during dorsal closure
    • Franke, J. D., Montague, R. A., and Kiehart, D. P. (2005) Nonmuscle myosin II generates forces that transmit tension and drive contraction in multiple tissues during dorsal closure. Curr. Biol. 15, 2208-2221
    • (2005) Curr. Biol , vol.15 , pp. 2208-2221
    • Franke, J.D.1    Montague, R.A.2    Kiehart, D.P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.