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Volumn 10, Issue , 2017, Pages

Post-translational modifications and protein quality control in motor neuron and polyglutamine diseases

Author keywords

Aggregation; Motor neuron disease; Polyglutamine disease; Post translational modifications; Protein degradation

Indexed keywords

ACTIVATING TRANSCRIPTION FACTOR 4; ANDROGEN RECEPTOR; ARGININE; ATAXIN 1; ATAXIN 2; ATAXIN 3; ATAXIN 7; CASEIN KINASE II; COPPER ZINC SUPEROXIDE DISMUTASE; CYCLIN DEPENDENT KINASE 5; GLYCOGEN SYNTHASE KINASE 3; GLYCOGEN SYNTHASE KINASE 3BETA; I KAPPA B KINASE; PARKIN; POLYGLUTAMINE; SIRTUIN 1; TAR DNA BINDING PROTEIN; VALOSIN CONTAINING PROTEIN;

EID: 85018909265     PISSN: 16625099     EISSN: None     Source Type: Journal    
DOI: 10.3389/fnmol.2017.00082     Document Type: Review
Times cited : (50)

References (135)
  • 1
    • 34248327285 scopus 로고    scopus 로고
    • CHIP overexpression reduces mutant androgen receptor protein and ameliorates phenotypes of the spinal and bulbar muscular atrophy transgenic mouse model
    • Adachi, H., Waza, M., Tokui, K., Katsuno, M., Minamiyama, M., Tanaka, F., et al. (2007). CHIP overexpression reduces mutant androgen receptor protein and ameliorates phenotypes of the spinal and bulbar muscular atrophy transgenic mouse model. J. Neurosci. 27, 5115–5126. doi: 10.1523/JNEUROSCI.1242-07.2007
    • (2007) J. Neurosci. , vol.27 , pp. 5115-5126
    • Adachi, H.1    Waza, M.2    Tokui, K.3    Katsuno, M.4    Minamiyama, M.5    Tanaka, F.6
  • 2
    • 70350380989 scopus 로고    scopus 로고
    • Phosphorylation of threonine 3: Implications for Huntingtin aggregation and neurotoxicity
    • Aiken, C. T., Steffan, J. S., Guerrero, C. M., Khashwji, H., Lukacsovich, T., Simmons, D., et al. (2009). Phosphorylation of threonine 3: implications for Huntingtin aggregation and neurotoxicity. J. Biol. Chem. 284, 29427–29436. doi: 10.1074/jbc.M109.013193
    • (2009) J. Biol. Chem. , vol.284 , pp. 29427-29436
    • Aiken, C.T.1    Steffan, J.S.2    Guerrero, C.M.3    Khashwji, H.4    Lukacsovich, T.5    Simmons, D.6
  • 3
    • 84955513053 scopus 로고    scopus 로고
    • SUMOylation of the brain-predominant Ataxin-3 isoform modulates its interaction with p97
    • Almeida, B., Abreu, I. A., Matos, C. A., Fraga, J. S., Fernandes, S., Macedo, M. G., et al. (2015). SUMOylation of the brain-predominant Ataxin-3 isoform modulates its interaction with p97. Biochim. Biophys. Acta 1852, 1950–1959. doi: 10.1016/j.bbadis.2015.06.010
    • (2015) Biochim. Biophys. Acta , vol.1852 , pp. 1950-1959
    • Almeida, B.1    Abreu, I.A.2    Matos, C.A.3    Fraga, J.S.4    Fernandes, S.5    Macedo, M.G.6
  • 4
    • 33748741301 scopus 로고    scopus 로고
    • CHIP protects from the neurotoxicity of expanded and wild-type ataxin-1 and promotes their ubiquitination and degradation
    • Al-Ramahi, I., Lam, Y. C., Chen, H. K., de Gouyon, B., Zhang, M., Perez, A. M., et al. (2006). CHIP protects from the neurotoxicity of expanded and wild-type ataxin-1 and promotes their ubiquitination and degradation. J. Biol. Chem. 281, 26714–26724. doi: 10.1074/jbc.M601603200
    • (2006) J. Biol. Chem. , vol.281 , pp. 26714-26724
    • Al-Ramahi, I.1    Lam, Y.C.2    Chen, H.K.3    De Gouyon, B.4    Zhang, M.5    Perez, A.M.6
  • 5
    • 84943543196 scopus 로고    scopus 로고
    • DYRK2 negatively regulates type I interferon induction by promoting TBK1 degradation via Ser527 phosphorylation
    • An, T., Li, S., Pan, W., Tien, P., Zhong, B., Shu, H. B., et al. (2015). DYRK2 negatively regulates type I interferon induction by promoting TBK1 degradation via Ser527 phosphorylation. PLoS Pathog. 11:e1005179. doi: 10.1371/journal.ppat.1005179
    • (2015) Plos Pathog , vol.11
    • An, T.1    Li, S.2    Pan, W.3    Tien, P.4    Zhong, B.5    Shu, H.B.6
  • 6
    • 14644437074 scopus 로고    scopus 로고
    • Transcriptional down-regulation through nuclear exclusion of EWS methylated by PRMT1
    • Araya, N., Hiraga, H., Kako, K., Arao, Y., Kato, S., and Fukamizu, A. (2005). Transcriptional down-regulation through nuclear exclusion of EWS methylated by PRMT1. Biochem. Biophys. Res. Commun. 329, 653–660. doi: 10.1016/j.bbrc.2005.02.018
    • (2005) Biochem. Biophys. Res. Commun. , vol.329 , pp. 653-660
    • Araya, N.1    Hiraga, H.2    Kako, K.3    Arao, Y.4    Kato, S.5    Fukamizu, A.6
  • 7
    • 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., and Finkbeiner, S. (2004). Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death. Nature 431, 805–810. doi: 10.1038/nature02998
    • (2004) Nature , vol.431 , pp. 805-810
    • Arrasate, M.1    Mitra, S.2    Schweitzer, E.S.3    Segal, M.R.4    Finkbeiner, S.5
  • 8
    • 84894065968 scopus 로고    scopus 로고
    • Cyclin-dependent kinase 5 phosphorylates and induces the degradation of ataxin-2
    • Asada, A., Yamazaki, R., Kino, Y., Saito, T., Kimura, T., Miyake, M., et al. (2014). Cyclin-dependent kinase 5 phosphorylates and induces the degradation of ataxin-2. Neurosci. Lett. 563, 112–117. doi: 10.1016/j.neulet.2014. 01.046
    • (2014) Neurosci. Lett. , vol.563 , pp. 112-117
    • Asada, A.1    Yamazaki, R.2    Kino, Y.3    Saito, T.4    Kimura, T.5    Miyake, M.6
  • 9
    • 84929650719 scopus 로고    scopus 로고
    • Serine phosphorylation and arginine methylation at the crossroads to neurodegeneration
    • Basso, M., and Pennuto, M. (2015). Serine phosphorylation and arginine methylation at the crossroads to neurodegeneration. Exp. Neurol. 271, 77–83. doi: 10.1016/j.expneurol.2015.05.003
    • (2015) Exp. Neurol. , vol.271 , pp. 77-83
    • Basso, M.1    Pennuto, M.2
  • 10
    • 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. doi: 10.1111/j.1471-4159.2004.02369.x
    • (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
  • 11
    • 85009809514 scopus 로고    scopus 로고
    • Arginine methylation: The coming of age
    • Blanc, R. S., and Richard, S. (2017). Arginine methylation: the coming of age. Mol. Cell 65, 8–24. doi: 10.1016/j.molcel.2016.11.003
    • (2017) Mol. Cell , vol.65 , pp. 8-24
    • Blanc, R.S.1    Richard, S.2
  • 12
    • 78650680776 scopus 로고    scopus 로고
    • Regulation of TDP-43 aggregation by phosphorylation and p62/SQSTM1
    • Brady, O. A., Meng, P., Zheng, Y., Mao, Y., and Hu, F. (2011). Regulation of TDP-43 aggregation by phosphorylation and p62/SQSTM1. J. Neurochem. 116, 248–259. doi: 10.1111/j.1471-4159.2010.07098.x
    • (2011) J. Neurochem. , vol.116 , pp. 248-259
    • Brady, O.A.1    Meng, P.2    Zheng, Y.3    Mao, Y.4    Hu, F.5
  • 13
    • 84920106094 scopus 로고    scopus 로고
    • TDP-43 modification in the hSOD1(G93A) amyotrophic lateral sclerosis mouse model
    • Cai, M., Lee, K. W., Choi, S. M., and Yang, E. J. (2015). TDP-43 modification in the hSOD1(G93A) amyotrophic lateral sclerosis mouse model. Neurol. Res. 37, 253–262. doi: 10.1179/1743132814Y.0000000443
    • (2015) Neurol. Res. , vol.37 , pp. 253-262
    • Cai, M.1    Lee, K.W.2    Choi, S.M.3    Yang, E.J.4
  • 14
    • 84979587970 scopus 로고    scopus 로고
    • Acetylation within the First 17 residues of Huntingtin exon 1 alters aggregation and lipid binding
    • Chaibva, M., Jawahery, S., Pilkington, A. W. IV, Arndt, J. R., Sarver, O., Valentine, S., et al. (2016). Acetylation within the First 17 residues of Huntingtin exon 1 alters aggregation and lipid binding. Biophys. J. 111, 349–362. doi: 10.1016/j.bpj.2016.06.018
    • (2016) Biophys. J. , vol.111 , pp. 349-362
    • Chaibva, M.1    Jawahery, S.2    Pilkington, A.W.3    Arndt, J.R.4    Sarver, O.5    Valentine, S.6
  • 15
    • 84936886629 scopus 로고    scopus 로고
    • Defective proteasome delivery of polyubiquitinated proteins by ubiquilin-2 proteins containing ALS mutations
    • Chang, L., and Monteiro, M. J. (2015). Defective proteasome delivery of polyubiquitinated proteins by ubiquilin-2 proteins containing ALS mutations. PLoS ONE 10:e0130162. doi: 10.1371/journal.pone.0130162
    • (2015) Plos ONE , vol.10
    • Chang, L.1    Monteiro, M.J.2
  • 16
    • 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., Fernandez-Funez, P., Acevedo, S. F., Lam, Y. C., Kaytor, M. D., Fernandez, M. H., et al. (2003). Interaction of Akt-phosphorylated ataxin-1 with 14-3-3 mediates neurodegeneration in spinocerebellar ataxia type 1. Cell 113, 457–468. doi: 10.1016/S0092-8674(03)00349-0
    • (2003) Cell , vol.113 , pp. 457-468
    • Chen, H.K.1    Fernandez-Funez, P.2    Acevedo, S.F.3    Lam, Y.C.4    Kaytor, M.D.5    Fernandez, M.H.6
  • 17
    • 0033912716 scopus 로고    scopus 로고
    • Minocycline inhibits caspase-1 and caspase-3 expression and delays mortality in a transgenic mouse model of Huntington disease
    • Chen, M., Ona, V. O., Li, M., Ferrante, R. J., Fink, K. B., Zhu, S., et al. (2000). Minocycline inhibits caspase-1 and caspase-3 expression and delays mortality in a transgenic mouse model of Huntington disease. Nat. Med. 6, 797–801. doi: 10.1038/80538
    • (2000) Nat. Med , vol.6 , pp. 797-801
    • Chen, M.1    Ona, V.O.2    Li, M.3    Ferrante, R.J.4    Fink, K.B.5    Zhu, S.6
  • 18
    • 33845864451 scopus 로고    scopus 로고
    • Co-chaperone CHIP promotes aggregation of ataxin-1
    • Choi, J. Y., Ryu, J. H., Kim, H. S., Park, S. G., Bae, K. H., Kang, S., et al. (2007). Co-chaperone CHIP promotes aggregation of ataxin-1. Mol. Cell. Neurosci. 34, 69–79. doi: 10.1016/j.mcn.2006.10.002
    • (2007) Mol. Cell. Neurosci. , vol.34 , pp. 69-79
    • Choi, J.Y.1    Ryu, J.H.2    Kim, H.S.3    Park, S.G.4    Bae, K.H.5    Kang, S.6
  • 19
    • 84893012138 scopus 로고    scopus 로고
    • TDP-43 Phosphorylation by casein kinase Iepsilon promotes oligomerizationand enhances toxicity invivo
    • Choksi, D. K., Roy, B., Chatterjee, S., Yusuff, T., Bakhoum, M. F., Sengupta, U., et al. (2014). TDP-43 Phosphorylation by casein kinase Iepsilon promotes oligomerizationand enhances toxicity invivo. Hum. Mol. Genet. 23, 1025–1035. doi: 10.1093/hmg/ddt498
    • (2014) Hum. Mol. Genet. , vol.23 , pp. 1025-1035
    • Choksi, D.K.1    Roy, B.2    Chatterjee, S.3    Yusuff, T.4    Bakhoum, M.F.5    Sengupta, U.6
  • 20
    • 84959852058 scopus 로고    scopus 로고
    • Disrupting SUMOylation enhances transcriptional function and ameliorates polyglutamine androgen receptor-mediated disease
    • Chua, J. P., Reddy, S. L., Yu, Z., Giorgetti, E., Montie, H. L., Mukherjee, S., et al. (2015). Disrupting SUMOylation enhances transcriptional function and ameliorates polyglutamine androgen receptor-mediated disease. J. Clin. Invest. 125, 831–845. doi: 10.1172/JCI73214
    • (2015) J. Clin. Invest. , vol.125 , pp. 831-845
    • Chua, J.P.1    Reddy, S.L.2    Yu, Z.3    Giorgetti, E.4    Montie, H.L.5    Mukherjee, S.6
  • 21
    • 84941786176 scopus 로고    scopus 로고
    • An acetylation switch controls TDP-43 function and aggregation propensity
    • Cohen, T. J., Hwang, A. W., Restrepo, C. R., Yuan, C. X., Trojanowski, J. Q., and Lee, V. M. (2015). An acetylation switch controls TDP-43 function and aggregation propensity. Nat. Commun. 6, 5845. doi: 10.1038/ncomms6845
    • (2015) Nat. Commun. , vol.6 , pp. 5845
    • Cohen, T.J.1    Hwang, A.W.2    Restrepo, C.R.3    Yuan, C.X.4    Trojanowski, J.Q.5    Lee, V.M.6
  • 22
    • 84948701265 scopus 로고    scopus 로고
    • Inhibition of pathogenic mutant SOD1 aggregation in cultured motor neuronal cells by prevention of its SUMOylation on lysine 75
    • Dangoumau, A., Marouillat, S., Burlaud Gaillard, J., Uzbekov, R., Veyrat-Durebex, C., Blasco, H., et al. (2016). Inhibition of pathogenic mutant SOD1 aggregation in cultured motor neuronal cells by prevention of its SUMOylation on lysine 75. Neurodegener. Dis. 16, 161–171. doi: 10.1159/000439254
    • (2016) Neurodegener. Dis , vol.16 , pp. 161-171
    • Dangoumau, A.1    Marouillat, S.2    Burlaud Gaillard, J.3    Uzbekov, R.4    Veyrat-Durebex, C.5    Blasco, H.6
  • 23
    • 0030752709 scopus 로고    scopus 로고
    • Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain
    • DiFiglia, M., Sapp, E., Chase, K. O., Davies, S. W., Bates, G. P., Vonsattel, J. P., et al. (1997). Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain. Science 277, 1990–1993. doi: 10.1126/science.277.5334.1990
    • (1997) Science , vol.277 , pp. 1990-1993
    • Difiglia, M.1    Sapp, E.2    Chase, K.O.3    Davies, S.W.4    Bates, G.P.5    Vonsattel, J.P.6
  • 24
    • 0042808497 scopus 로고    scopus 로고
    • Ubiquitin-mediated sequestration of normal cellular proteins into polyglutamine aggregates
    • Donaldson, K. M., Li, W., Ching, K. A., Batalov, S., Tsai, C. C., and Joazeiro, C. A. (2003). Ubiquitin-mediated sequestration of normal cellular proteins into polyglutamine aggregates. Proc. Natl. Acad. Sci. U.S.A. 100, 8892–8897. doi: 10.1073/pnas.1530212100
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 8892-8897
    • Donaldson, K.M.1    Li, W.2    Ching, K.A.3    Batalov, S.4    Tsai, C.C.5    Joazeiro, C.A.6
  • 25
    • 67650432367 scopus 로고    scopus 로고
    • Proteolytic processing of TAR DNA binding protein-43 by caspases produces C-terminal fragments with disease defining properties independent of progranulin
    • Dormann, D., Capell, A., Carlson, A. M., Shankaran, S. S., Rodde, R., Neumann, M., et al. (2009). Proteolytic processing of TAR DNA binding protein-43 by caspases produces C-terminal fragments with disease defining properties independent of progranulin. J. Neurochem. 110, 1082–1094. doi: 10.1111/j.1471-4159.2009.06211.x
    • (2009) J. Neurochem. , vol.110 , pp. 1082-1094
    • Dormann, D.1    Capell, A.2    Carlson, A.M.3    Shankaran, S.S.4    Rodde, R.5    Neumann, M.6
  • 26
    • 84869237956 scopus 로고    scopus 로고
    • Arginine methylation next to the PY-NLS modulates transportin binding and nuclear import of FUS
    • Dormann, D., Madl, T., Valori, C. F., Bentmann, E., Tahirovic, S., Abou-Ajram, C., et al. (2012). Arginine methylation next to the PY-NLS modulates transportin binding and nuclear import of FUS. EMBO J. 31, 4258–4275. doi: 10.1038/emboj.2012.261
    • (2012) EMBO J , vol.31 , pp. 4258-4275
    • Dormann, D.1    Madl, T.2    Valori, C.F.3    Bentmann, E.4    Tahirovic, S.5    Abou-Ajram, C.6
  • 27
    • 79151471350 scopus 로고    scopus 로고
    • TLS and PRMT1 synergistically coactivate transcription at the survivin promoter through TLS arginine methylation
    • Du, K., Arai, S., Kawamura, T., Matsushita, A., and Kurokawa, R. (2011). TLS and PRMT1 synergistically coactivate transcription at the survivin promoter through TLS arginine methylation. Biochem. Biophys. Res. Commun. 404, 991–996. doi: 10.1016/j.bbrc.2010.12.097
    • (2011) Biochem. Biophys. Res. Commun. , vol.404 , pp. 991-996
    • Du, K.1    Arai, S.2    Kawamura, T.3    Matsushita, A.4    Kurokawa, R.5
  • 29
    • 0033605746 scopus 로고    scopus 로고
    • Cleavage of atrophin-1 at caspase site aspartic acid 109 modulates cytotoxicity
    • Ellerby, L. M., Andrusiak, R. L., Wellington, C. L., Hackam, A. S., Propp, S. S., Wood, J. D., et al. (1999a). Cleavage of atrophin-1 at caspase site aspartic acid 109 modulates cytotoxicity. J. Biol. Chem. 274, 8730–8736. doi: 10.1074/jbc.274.13.8730
    • (1999) J. Biol. Chem. , vol.274 , pp. 8730-8736
    • Ellerby, L.M.1    Andrusiak, R.L.2    Wellington, C.L.3    Hackam, A.S.4    Propp, S.S.5    Wood, J.D.6
  • 30
    • 0032898311 scopus 로고    scopus 로고
    • Kennedy’s disease: Caspase cleavage of the androgen receptor is a crucial event in cytotoxicity
    • Ellerby, L. M., Hackam, A. S., Propp, S. S., Ellerby, H. M., Rabizadeh, S., Cashman, N. R., et al. (1999b). Kennedy’s disease: caspase cleavage of the androgen receptor is a crucial event in cytotoxicity. J. Neurochem. 72, 185–195. doi: 10.1046/j.1471-4159.1999.0720185.x
    • (1999) J. Neurochem. , vol.72 , pp. 185-195
    • Ellerby, L.M.1    Hackam, A.S.2    Propp, S.S.3    Ellerby, H.M.4    Rabizadeh, S.5    Cashman, N.R.6
  • 31
    • 84993968490 scopus 로고    scopus 로고
    • A phosphomimetic mutation stabilizes SOD1 and rescues cell viability in the context of an ALS-associated mutation
    • Fay, J. M., Zhu, C., Proctor, E. A., Tao, Y., Cui, W., Ke, H., et al. (2016). A phosphomimetic mutation stabilizes SOD1 and rescues cell viability in the context of an ALS-associated mutation. Structure 24, 1898–1906. doi: 10.1016/j.str.2016.08.011
    • (2016) Structure , vol.24 , pp. 1898-1906
    • Fay, J.M.1    Zhu, C.2    Proctor, E.A.3    Tao, Y.4    Cui, W.5    Ke, H.6
  • 32
    • 33745924415 scopus 로고    scopus 로고
    • SUMO-1 modification increases human SOD1 stability and aggregation
    • Fei, E., Jia, N., Yan, M., Ying, Z., Sun, Q., Wang, H., et al. (2006). SUMO-1 modification increases human SOD1 stability and aggregation. Biochem. Biophys. Res. Commun. 347, 406–412. doi: 10.1016/j.bbrc.2006.06.092
    • (2006) Biochem. Biophys. Res. Commun. , vol.347 , pp. 406-412
    • Fei, E.1    Jia, N.2    Yan, M.3    Ying, Z.4    Sun, Q.5    Wang, H.6
  • 33
    • 34247160537 scopus 로고    scopus 로고
    • Phosphorylation of ataxin-3 by glycogen synthase kinase 3beta at serine 256 regulates the aggregation of ataxin-3
    • Fei, E., Jia, N., Zhang, T., Ma, X., Wang, H., Liu, C., et al. (2007). Phosphorylation of ataxin-3 by glycogen synthase kinase 3beta at serine 256 regulates the aggregation of ataxin-3. Biochem. Biophys. Res. Commun. 357, 487–492. doi: 10.1016/j.bbrc.2007.03.160
    • (2007) Biochem. Biophys. Res. Commun. , vol.357 , pp. 487-492
    • Fei, E.1    Jia, N.2    Zhang, T.3    Ma, X.4    Wang, H.5    Liu, C.6
  • 34
    • 0142157600 scopus 로고    scopus 로고
    • Histone deacetylase inhibition by sodium butyrate chemotherapy ameliorates the neurodegenerative phenotype in Huntington’s disease mice
    • Ferrante, R. J., Kubilus, J. K., Lee, J., Ryu, H., Beesen, A., Zucker, B., et al. (2003). Histone deacetylase inhibition by sodium butyrate chemotherapy ameliorates the neurodegenerative phenotype in Huntington’s disease mice. J. Neurosci. 23, 9418–9427.
    • (2003) J. Neurosci. , vol.23 , pp. 9418-9427
    • Ferrante, R.J.1    Kubilus, J.K.2    Lee, J.3    Ryu, H.4    Beesen, A.5    Zucker, B.6
  • 35
    • 84878944582 scopus 로고    scopus 로고
    • Sumoylation: A regulatory protein modification in health and disease
    • Flotho, A., and Melchior, F. (2013). Sumoylation: a regulatory protein modification in health and disease. Annu. Rev. Biochem. 82, 357–385. doi: 10.1146/annurev-biochem-061909-093311
    • (2013) Annu. Rev. Biochem. , vol.82 , pp. 357-385
    • Flotho, A.1    Melchior, F.2
  • 36
    • 0034617058 scopus 로고    scopus 로고
    • P300 and p300/cAMP-response element-binding protein-associated factor acetylate the androgen receptor at sites governing hormone-dependent transactivation
    • Fu, M., Wang, C., Reutens, A. T., Wang, J., Angeletti, R. H., Siconolfi-Baez, L., et al. (2000). p300 and p300/cAMP-response element-binding protein-associated factor acetylate the androgen receptor at sites governing hormone-dependent transactivation. J. Biol. Chem. 275, 20853–20860. doi: 10.1074/jbc.M000 660200
    • (2000) J. Biol. Chem. , vol.275 , pp. 20853-20860
    • Fu, M.1    Wang, C.2    Reutens, A.T.3    Wang, J.4    Angeletti, R.H.5    Siconolfi-Baez, L.6
  • 37
    • 84948158259 scopus 로고    scopus 로고
    • Treatment with a global methyltransferase inhibitor induces the intranuclear aggregation of ALS-linked FUS mutant in vitro
    • Fujii, S., Takanashi, K., Kitajo, K., and Yamaguchi, A. (2016). Treatment with a global methyltransferase inhibitor induces the intranuclear aggregation of ALS-linked FUS mutant in vitro. Neurochem. Res. 41, 826–835. doi: 10.1007/s11064-015-1758-z
    • (2016) Neurochem. Res. , vol.41 , pp. 826-835
    • Fujii, S.1    Takanashi, K.2    Kitajo, K.3    Yamaguchi, A.4
  • 38
    • 0037096376 scopus 로고    scopus 로고
    • Calpain activation in Huntington’s disease
    • Gafni, J., and Ellerby, L. M. (2002). Calpain activation in Huntington’s disease. J. Neurosci. 22, 4842–4849.
    • (2002) J. Neurosci. , vol.22 , pp. 4842-4849
    • Gafni, J.1    Ellerby, L.M.2
  • 39
    • 2442631459 scopus 로고    scopus 로고
    • Inhibition of calpain cleavage of huntingtin reduces toxicity: Accumulation of calpain/caspase fragments in the nucleus
    • Gafni, J., Hermel, E., Young, J. E., Wellington, C. L., Hayden, M. R., and Ellerby, L. M. (2004). Inhibition of calpain cleavage of huntingtin reduces toxicity: accumulation of calpain/caspase fragments in the nucleus. J. Biol. Chem. 279, 20211–20220. doi: 10.1074/jbc.M401267200
    • (2004) J. Biol. Chem. , vol.279 , pp. 20211-20220
    • Gafni, J.1    Hermel, E.2    Young, J.E.3    Wellington, C.L.4    Hayden, M.R.5    Ellerby, L.M.6
  • 40
    • 0037096365 scopus 로고    scopus 로고
    • Polyglutamine-expandedataxin-7 promotes non-cell-autonomous purkinje cell degeneration and displays proteolytic cleavage in ataxic transgenic mice
    • Garden, G. A., Libby, R. T., Fu, Y. H., Kinoshita, Y., Huang, J., Possin, D. E., et al. (2002). Polyglutamine-expandedataxin-7 promotes non-cell-autonomous purkinje cell degeneration and displays proteolytic cleavage in ataxic transgenic mice. J. Neurosci. 22, 4897–4905.
    • (2002) J. Neurosci , vol.22 , pp. 4897-4905
    • Garden, G.A.1    Libby, R.T.2    Fu, Y.H.3    Kinoshita, Y.4    Huang, J.5    Possin, D.E.6
  • 41
    • 19944431703 scopus 로고    scopus 로고
    • Neuroprotective effects of phenylbutyrate in the N171-82Q transgenic mouse model of Huntington’s disease
    • Gardian, G., Browne, S. E., Choi, D. K., Klivenyi, P., Gregorio, J., Kubilus, J. K., et al. (2005). Neuroprotective effects of phenylbutyrate in the N171-82Q transgenic mouse model of Huntington’s disease. J. Biol. Chem. 280, 556–563. doi: 10.1074/jbc.M410210200
    • (2005) J. Biol. Chem. , vol.280 , pp. 556-563
    • Gardian, G.1    Browne, S.E.2    Choi, D.K.3    Klivenyi, P.4    Gregorio, J.5    Kubilus, J.K.6
  • 42
    • 23244449018 scopus 로고    scopus 로고
    • Activation of NMDAreceptors induces protein kinase A-mediated phosphorylation and degradation of matrin 3. Blocking these effects prevents NMDA-induced neuronal death
    • Giordano, G., Sanchez-Perez, A. M., Montoliu, C., Berezney, R., Malyavantham, K., Costa, L. G., et al. (2005). Activation of NMDAreceptors induces protein kinase A-mediated phosphorylation and degradation of matrin 3. Blocking these effects prevents NMDA-induced neuronal death. J. Neurochem. 94, 808–818. doi: 10.1111/j.1471-4159.2005.03235.x
    • (2005) J. Neurochem. , vol.94 , pp. 808-818
    • Giordano, G.1    Sanchez-Perez, A.M.2    Montoliu, C.3    Berezney, R.4    Malyavantham, K.5    Costa, L.G.6
  • 43
    • 9344227302 scopus 로고    scopus 로고
    • Cleavage of huntingtin by apopain, a proapoptotic cysteine protease, is modulated by the polyglutamine tract
    • Goldberg, Y. P., Nicholson, D. W., Rasper, D. M., Kalchman, M. A., Koide, H. B., Graham, R. K., et al. (1996). Cleavage of huntingtin by apopain, a proapoptotic cysteine protease, is modulated by the polyglutamine tract. Nat. Genet. 13, 442–449. doi: 10.1038/ng0896-442
    • (1996) Nat. Genet. , vol.13 , pp. 442-449
    • Goldberg, Y.P.1    Nicholson, D.W.2    Rasper, D.M.3    Kalchman, M.A.4    Koide, H.B.5    Graham, R.K.6
  • 44
    • 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., et al. (2006). Cleavage at the caspase-6 site is required for neuronal dysfunction and degeneration due to mutant huntingtin. Cell 125, 1179–1191. doi: 10.1016/j.cell.2006.04.026
    • (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
  • 45
    • 72149107077 scopus 로고    scopus 로고
    • Serines 13 and 16 are critical determinants of full-length human mutant huntingtin induced disease pathogenesis in HD mice
    • Gu, X., Greiner, E. R., Mishra, R., Kodali, R., Osmand, A., Finkbeiner, S., et al. (2009). Serines 13 and 16 are critical determinants of full-length human mutant huntingtin induced disease pathogenesis in HD mice. Neuron 64, 828–840. doi: 10.1016/j.neuron.2009.11.020
    • (2009) Neuron , vol.64 , pp. 828-840
    • Gu, X.1    Greiner, E.R.2    Mishra, R.3    Kodali, R.4    Osmand, A.5    Finkbeiner, S.6
  • 46
    • 32144436256 scopus 로고    scopus 로고
    • Proteolytic cleavage of polyglutamine-expanded ataxin-3 is critical for aggregation and sequestration of non-expanded ataxin-3
    • Haacke, A., Broadley, S. A., Boteva, R., Tzvetkov, N., Hartl, F. U., and Breuer, P. (2006). Proteolytic cleavage of polyglutamine-expanded ataxin-3 is critical for aggregation and sequestration of non-expanded ataxin-3. Hum. Mol. Genet. 15, 555–568. doi: 10.1093/hmg/ddi472
    • (2006) Hum. Mol. Genet. , vol.15 , pp. 555-568
    • Haacke, A.1    Broadley, S.A.2    Boteva, R.3    Tzvetkov, N.4    Hartl, F.U.5    Breuer, P.6
  • 47
    • 84903851882 scopus 로고    scopus 로고
    • UBE2E ubiquitin-conjugating enzymes and ubiquitin isopeptidase Y regulate TDP-43 protein ubiquitination
    • Hans, F., Fiesel, F. C., Strong, J. C., Jackel, S., Rasse, T. M., Geisler, S., et al. (2014). UBE2E ubiquitin-conjugating enzymes and ubiquitin isopeptidase Y regulate TDP-43 protein ubiquitination. J. Biol. Chem. 289, 19164–19179. doi: 10.1074/jbc.M114.561704
    • (2014) J. Biol. Chem. , vol.289 , pp. 19164-19179
    • Hans, F.1    Fiesel, F.C.2    Strong, J.C.3    Jackel, S.4    Rasse, T.M.5    Geisler, S.6
  • 48
    • 47949086625 scopus 로고    scopus 로고
    • Phosphorylated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis
    • Hasegawa, M., Arai, T., Nonaka, T., Kametani, F., Yoshida, M., Hashizume, Y., et al. (2008). Phosphorylated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis. Ann. Neurol. 64, 60–70. doi: 10.1002/ana. 21425
    • (2008) Ann. Neurol. , vol.64 , pp. 60-70
    • Hasegawa, M.1    Arai, T.2    Nonaka, T.3    Kametani, F.4    Yoshida, M.5    Hashizume, Y.6
  • 49
    • 84873615689 scopus 로고    scopus 로고
    • Parkin ubiquitinates Tar-DNA binding protein-43 (TDP-43) and promotes its cytosolic accumulation via interaction with histone deacetylase 6 (HDAC6)
    • Hebron, M. L., Lonskaya, I., Sharpe, K., Weerasinghe, P. P., Algarzae, N. K., Shekoyan, A. R., et al. (2013). Parkin ubiquitinates Tar-DNA binding protein-43 (TDP-43) and promotes its cytosolic accumulation via interaction with histone deacetylase 6 (HDAC6). J. Biol. Chem. 288, 4103–4115. doi: 10.1074/jbc.M112.419945
    • (2013) J. Biol. Chem. , vol.288 , pp. 4103-4115
    • Hebron, M.L.1    Lonskaya, I.2    Sharpe, K.3    Weerasinghe, P.P.4    Algarzae, N.K.5    Shekoyan, A.R.6
  • 50
    • 84897994248 scopus 로고    scopus 로고
    • Parkin reverses TDP-43-induced cell death and failure of amino acid homeostasis
    • Hebron, M., Chen, W., Miessau, M. J., Lonskaya, I., and Moussa, C. E. (2014). Parkin reverses TDP-43-induced cell death and failure of amino acid homeostasis. J. Neurochem. 129, 350–361. doi: 10.1111/jnc.12630
    • (2014) J. Neurochem. , vol.129 , pp. 350-361
    • Hebron, M.1    Chen, W.2    Miessau, M.J.3    Lonskaya, I.4    Moussa, C.E.5
  • 51
    • 11144357398 scopus 로고    scopus 로고
    • Specific caspase interactions and amplification are involved in selective neuronal vulnerability in Huntington’s disease
    • Hermel, E., Gafni, J., Propp, S. S., Leavitt, B. R., Wellington, C. L., Young, J. E., Hackam, A. S., et al. (2004). Specific caspase interactions and amplification are involved in selective neuronal vulnerability in Huntington’s disease. Cell Death Differ. 11, 424–438. doi: 10.1038/sj.cdd.4401358
    • (2004) Cell Death Differ , vol.11 , pp. 424-438
    • Hermel, E.1    Gafni, J.2    Propp, S.S.3    Leavitt, B.R.4    Wellington, C.L.5    Young, J.E.6    Hackam, A.S.7
  • 52
    • 0037452775 scopus 로고    scopus 로고
    • Suberoylanilide hydroxamic acid, a histone deacetylase inhibitor, ameliorates motor deficits ina mouse model of Huntington’s disease
    • Hockly, E., Richon, V. M., Woodman, B., Smith, D. L., Zhou, X., Rosa, E., et al. (2003). Suberoylanilide hydroxamic acid, a histone deacetylase inhibitor, ameliorates motor deficits ina mouse model of Huntington’s disease. Proc. Natl. Acad. Sci. U.S.A. 100, 2041–2046. doi: 10.1073/pnas.0437870100
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 2041-2046
    • Hockly, E.1    Richon, V.M.2    Woodman, B.3    Smith, D.L.4    Zhou, X.5    Rosa, E.6
  • 53
    • 0036083379 scopus 로고    scopus 로고
    • The IGF-1/Akt pathway is neuroprotective in Huntington’s disease and involves Huntingtin phosphorylation by Akt
    • Humbert, S., Bryson, E. A., Cordelieres, F. P., Connors, N. C., Datta, S. R., Finkbeiner, S., et al. (2002). The IGF-1/Akt pathway is neuroprotective in Huntington’s disease and involves Huntingtin phosphorylation by Akt. Dev. Cell 2, 831–837. doi: 10.1016/S1534-5807(02)00188-0
    • (2002) Dev. Cell , vol.2 , pp. 831-837
    • Humbert, S.1    Bryson, E.A.2    Cordelieres, F.P.3    Connors, N.C.4    Datta, S.R.5    Finkbeiner, S.6
  • 54
    • 48749088629 scopus 로고    scopus 로고
    • Abnormal phosphorylation of Ser409/410 of TDP-43 in FTLD-U and ALS
    • Inukai, Y., Nonaka, T., Arai, T., Yoshida, M., Hashizume, Y., Beach, T. G., et al. (2008). Abnormal phosphorylation of Ser409/410 of TDP-43 in FTLD-U and ALS. FEBS Lett. 582, 2899–2904. doi: 10.1016/j.febslet.2008.07.027
    • (2008) FEBS Lett , vol.582 , pp. 2899-2904
    • Inukai, Y.1    Nonaka, T.2    Arai, T.3    Yoshida, M.4    Hashizume, Y.5    Beach, T.G.6
  • 55
    • 15744387323 scopus 로고    scopus 로고
    • Co-chaperone CHIP associates with expanded polyglutamine protein and promotes their degradation by proteasomes
    • Jana, N. R., Dikshit, P., Goswami, A., Kotliarova, S., Murata, S., Tanaka, K., et al. (2005). Co-chaperone CHIP associates with expanded polyglutamine protein and promotes their degradation by proteasomes. J. Biol. Chem. 280, 11635–11640. doi: 10.1074/jbc.M412042200
    • (2005) J. Biol. Chem. , vol.280 , pp. 11635-11640
    • Jana, N.R.1    Dikshit, P.2    Goswami, A.3    Kotliarova, S.4    Murata, S.5    Tanaka, K.6
  • 56
    • 77649186048 scopus 로고    scopus 로고
    • SUMOylation attenuates the aggregation propensity and cellular toxicity of the polyglutamine expanded ataxin-7
    • Janer, A., Werner, A., Takahashi-Fujigasaki, J., Daret, A., Fujigasaki, H., Takada, K., et al. (2010). SUMOylation attenuates the aggregation propensity and cellular toxicity of the polyglutamine expanded ataxin-7. Hum. Mol. Genet. 19, 181–195. doi: 10.1093/hmg/ddp478
    • (2010) Hum. Mol. Genet. , vol.19 , pp. 181-195
    • Janer, A.1    Werner, A.2    Takahashi-Fujigasaki, J.3    Daret, A.4    Fujigasaki, H.5    Takada, K.6
  • 57
    • 63049132756 scopus 로고    scopus 로고
    • Acetylation targets mutant huntingtin to autophagosomes for degradation
    • Jeong, H., Then, F., Melia, T. J. Jr., Mazzulli, J. R., Cui, L., Savas, J. N., et al. (2009). Acetylation targets mutant huntingtin to autophagosomes for degradation. Cell 137, 60–72. doi: 10.1016/j.cell.2009.03.018
    • (2009) Cell , vol.137 , pp. 60-72
    • Jeong, H.1    Then, F.2    Melia, T.J.3    Mazzulli, J.R.4    Cui, L.5    Savas, J.N.6
  • 58
    • 84870378784 scopus 로고    scopus 로고
    • Selective histone deacetylase (HDAC) inhibition imparts beneficial effects in Huntington’s disease mice: Implications for the ubiquitin-proteasomal and autophagy systems
    • Jia, H., Kast, R. J., Steffan, J. S., and Thomas, E. A. (2012). Selective histone deacetylase (HDAC) inhibition imparts beneficial effects in Huntington’s disease mice: implications for the ubiquitin-proteasomal and autophagy systems. Hum. Mol. Genet. 21, 5280–5293. doi: 10.1093/hmg/dds379
    • (2012) Hum. Mol. Genet. , vol.21 , pp. 5280-5293
    • Jia, H.1    Kast, R.J.2    Steffan, J.S.3    Thomas, E.A.4
  • 59
    • 63049100536 scopus 로고    scopus 로고
    • PRMT1 mediated methylation of TAF15 is required for its positive gene regulatory function
    • Jobert, L., Argentini, M., and Tora, L. (2009). PRMT1 mediated methylation of TAF15 is required for its positive gene regulatory function. Exp. Cell Res. 315, 1273–1286. doi: 10.1016/j.yexcr.2008.12.008
    • (2009) Exp. Cell Res. , vol.315 , pp. 1273-1286
    • Jobert, L.1    Argentini, M.2    Tora, L.3
  • 61
    • 53049097189 scopus 로고    scopus 로고
    • EWS is a substrate of type I protein arginine methyltransferase, PRMT8
    • Kim, J.-D., Kako, K., Kakiuchi, M., Park, G. G., and Fukamizu, A. (2008). EWS is a substrate of type I protein arginine methyltransferase, PRMT8. Int. J. Mol. Med. 22, 309–315. doi: 10.3892/ijmm_00000024
    • (2008) Int. J. Mol. Med , vol.22 , pp. 309-315
    • Kim, J.-D.1    Kako, K.2    Kakiuchi, M.3    Park, G.G.4    Fukamizu, A.5
  • 62
    • 65549084887 scopus 로고    scopus 로고
    • Potentiation of amyotrophic lateral sclerosis (ALS)-associated TDP-43 aggregation by the proteasome-targeting factor, ubiquilin 1
    • Kim, S. H., Shi, Y., Hanson, K. A., Williams, L. M., Sakasai, R., Bowler, M. J., et al. (2009). Potentiation of amyotrophic lateral sclerosis (ALS)-associated TDP-43 aggregation by the proteasome-targeting factor, ubiquilin 1. J. Biol. Chem. 284, 8083–8092. doi: 10.1074/jbc.M808064200
    • (2009) J. Biol. Chem. , vol.284 , pp. 8083-8092
    • Kim, S.H.1    Shi, Y.2    Hanson, K.A.3    Williams, L.M.4    Sakasai, R.5    Bowler, M.J.6
  • 63
    • 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., et al. (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. U.S.A. 98, 12784–12789. doi: 10.1073/pnas.221451398
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , 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
  • 64
    • 84987836134 scopus 로고    scopus 로고
    • Serine 421 regulates mutant huntingtin toxicity and clearance in mice
    • Kratter, I. H., Zahed, H., Lau, A., Tsvetkov, A. S., Daub, A. C., Weiberth, K. F., et al. (2016). Serine 421 regulates mutant huntingtin toxicity and clearance in mice. J. Clin. Invest. 126, 3585–3597. doi: 10.1172/JCI80339
    • (2016) J. Clin. Invest. , vol.126 , pp. 3585-3597
    • Kratter, I.H.1    Zahed, H.2    Lau, A.3    Tsvetkov, A.S.4    Daub, A.C.5    Weiberth, K.F.6
  • 65
    • 0041816369 scopus 로고    scopus 로고
    • Kennedy’s disease. Phosphorylation of the polyglutamine-expanded form of androgen receptor regulates its cleavage by caspase-3 and enhances cell death
    • LaFevre-Bernt, M. A., and Ellerby, L. M. (2003). Kennedy’s disease. Phosphorylation of the polyglutamine-expanded form of androgen receptor regulates its cleavage by caspase-3 and enhances cell death. J. Biol. Chem. 278, 34918–34924. doi: 10.1074/jbc.M302841200
    • (2003) J. Biol. Chem. , vol.278 , pp. 34918-34924
    • Lafevre-Bernt, M.A.1    Ellerby, L.M.2
  • 66
    • 79961148135 scopus 로고    scopus 로고
    • Hyperphosphorylation as a defense mechanismto reduce TDP-43 aggregation
    • Li, H. Y., Yeh, P. A., Chiu, H. C., Tang, C. Y., and Tu, B. P. (2011). Hyperphosphorylation as a defense mechanismto reduce TDP-43 aggregation. PLoS ONE 6:e23075. doi: 10.1371/journal.pone.0023075
    • (2011) Plos ONE , vol.6
    • Li, H.Y.1    Yeh, P.A.2    Chiu, H.C.3    Tang, C.Y.4    Tu, B.P.5
  • 67
    • 78649750391 scopus 로고    scopus 로고
    • Phosphorylation promotes neurotoxicity in a Caenorhabditis elegans model of TDP-43 proteinopathy
    • Liachko, N. F., Guthrie, C. R., and Kraemer, B. C. (2010). Phosphorylation promotes neurotoxicity in a Caenorhabditis elegans model of TDP-43 proteinopathy. J. Neurosci. 30, 16208–16219. doi: 10.1523/JNEUROSCI. 2911-10.2010
    • (2010) J. Neurosci , vol.30 , pp. 16208-16219
    • Liachko, N.F.1    Guthrie, C.R.2    Kraemer, B.C.3
  • 68
    • 84883297079 scopus 로고    scopus 로고
    • CDC7 inhibition blocks pathological TDP-43 phosphorylation and neurodegeneration
    • Liachko, N. F., McMillan, P. J., Guthrie, C. R., Bird, T. D., Leverenz, J. B., and Kraemer, B. C. (2013). CDC7 inhibition blocks pathological TDP-43 phosphorylation and neurodegeneration. Ann. Neurol. 74, 39–52. doi: 10.1002/ana.23870
    • (2013) Ann. Neurol. , vol.74 , pp. 39-52
    • Liachko, N.F.1    McMillan, P.J.2    Guthrie, C.R.3    Bird, T.D.4    Leverenz, J.B.5    Kraemer, B.C.6
  • 69
    • 84919663858 scopus 로고    scopus 로고
    • The tau tubulin kinases TTBK1/2 promote accumulation of pathological TDP-43
    • Liachko, N. F., McMillan, P. J., Strovas, T. J., Loomis, E., Greenup, L., Murrell, J. R., et al. (2014). The tau tubulin kinases TTBK1/2 promote accumulation of pathological TDP-43. PLoS Genet. 10:e1004803. doi: 10.1371/journal. pgen.1004803
    • (2014) Plos Genet , vol.10
    • Liachko, N.F.1    McMillan, P.J.2    Strovas, T.J.3    Loomis, E.4    Greenup, L.5    Murrell, J.R.6
  • 70
    • 84980017377 scopus 로고    scopus 로고
    • The phosphatase calcineurin regulates pathological TDP-43 phosphorylation
    • Liachko, N. F., Saxton, A. D., McMillan, P. J., Strovas, T. J., Currey, H. N., Taylor, L. M., et al. (2016). The phosphatase calcineurin regulates pathological TDP-43 phosphorylation. Acta Neuropathol. 132, 545–561. doi: 10.1007/s00401-016-1600-y
    • (2016) Acta Neuropathol , vol.132 , pp. 545-561
    • Liachko, N.F.1    Saxton, A.D.2    McMillan, P.J.3    Strovas, T.J.4    Currey, H.N.5    Taylor, L.M.6
  • 71
    • 0037101834 scopus 로고    scopus 로고
    • Altered transcriptional regulation in cells expressing the expanded polyglutamine androgen receptor
    • Lieberman, A. P., Harmison, G., Strand, A. D., Olson, J. M., and Fischbeck, K. H. (2002). Altered transcriptional regulation in cells expressing the expanded polyglutamine androgen receptor. Hum. Mol. Genet. 11, 1967–1976. doi: 10.1093/hmg/11.17.1967
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 1967-1976
    • Lieberman, A.P.1    Harmison, G.2    Strand, A.D.3    Olson, J.M.4    Fischbeck, K.H.5
  • 72
    • 0035912833 scopus 로고    scopus 로고
    • Akt suppresses androgen-induced apoptosis by phosphorylating and inhibiting androgen receptor
    • Lin, H. K., Yeh, S., Kang, H. Y., and Chang, C. (2001). Akt suppresses androgen-induced apoptosis by phosphorylating and inhibiting androgen receptor. Proc. Natl. Acad. Sci. U.S.A. 98, 7200–7205. doi: 10.1073/pnas.121173298
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 7200-7205
    • Lin, H.K.1    Yeh, S.2    Kang, H.Y.3    Chang, C.4
  • 73
    • 0036671821 scopus 로고    scopus 로고
    • Proteases acting on mutant huntingtin generate cleaved products that differentially build up cytoplasmic and nuclear inclusions
    • Lunkes, A., Lindenberg, K. S., Ben-Haiem, L., Weber, C., Devys, D., Landwehrmeyer, G. B., et al. (2002). Proteases acting on mutant huntingtin generate cleaved products that differentially build up cytoplasmic and nuclear inclusions. Mol. Cell 10, 259–269. doi: 10.1016/S1097-2765(02)00602-0
    • (2002) Mol. Cell , vol.10 , pp. 259-269
    • Lunkes, A.1    Lindenberg, K.S.2    Ben-Haiem, L.3    Weber, C.4    Devys, D.5    Landwehrmeyer, G.B.6
  • 74
    • 22344439156 scopus 로고    scopus 로고
    • Cdk5 phosphorylation of huntingtin reduces its cleavage by caspases: Implications for mutant huntingtin toxicity
    • Luo, S., Vacher, C., Davies, J. E., and Rubinsztein, D. C. (2005). Cdk5 phosphorylation of huntingtin reduces its cleavage by caspases: implications for mutant huntingtin toxicity. J. Cell Biol. 169, 647–656. doi: 10.1083/jcb.200412071
    • (2005) J. Cell Biol. , vol.169 , pp. 647-656
    • Luo, S.1    Vacher, C.2    Davies, J.E.3    Rubinsztein, D.C.4
  • 75
    • 70649108817 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors and neurodegenerative disorders: Holding the promise
    • Mai, A., Rotili, D., Valente, S., and Kazantsev, A. G. (2009). Histone deacetylase inhibitors and neurodegenerative disorders: holding the promise. Curr. Pharm. Des. 15, 3940–3957. doi: 10.2174/138161209789649349
    • (2009) Curr. Pharm. Des. , vol.15 , pp. 3940-3957
    • Mai, A.1    Rotili, D.2    Valente, S.3    Kazantsev, A.G.4
  • 76
    • 84959536774 scopus 로고    scopus 로고
    • Ataxin-3 phosphorylation decreases neuronal defects in spinocerebellar ataxia type 3 models
    • Matos, C. A., Nobrega, C., Louros, S. R., Almeida, B., Ferreiro, E., Valero, J., et al. (2016). Ataxin-3 phosphorylation decreases neuronal defects in spinocerebellar ataxia type 3 models. J. Cell Biol. 212, 465–480. doi: 10.1083/jcb.201 506025
    • (2016) J. Cell Biol. , vol.212 , pp. 465-480
    • Matos, C.A.1    Nobrega, C.2    Louros, S.R.3    Almeida, B.4    Ferreiro, E.5    Valero, J.6
  • 77
    • 1442264782 scopus 로고    scopus 로고
    • Molecular clearance of ataxin-3 is regulated by a mammalian E4
    • Matsumoto, M., Yada, M., Hatakeyama, S., Ishimoto, H., Tanimura, T., Tsuji, S., et al. (2004). Molecular clearance of ataxin-3 is regulated by a mammalian E4. EMBOJ. 23, 659–669. doi: 10.1038/sj.emboj.7600081
    • (2004) EMBOJ , vol.23 , pp. 659-669
    • Matsumoto, M.1    Yada, M.2    Hatakeyama, S.3    Ishimoto, H.4    Tanimura, T.5    Tsuji, S.6
  • 79
    • 2942733520 scopus 로고    scopus 로고
    • Sodium butyrate ameliorates phenotypic expression in a transgenic mouse model of spinal and bulbar muscular atrophy
    • Minamiyama, M., Katsuno, M., Adachi, H., Waza, M., Sang, C., Kobayashi, Y., et al. (2004). Sodium butyrate ameliorates phenotypic expression in a transgenic mouse model of spinal and bulbar muscular atrophy. Hum. Mol. Genet. 13, 1183–1192. doi: 10.1093/hmg/ddh131
    • (2004) Hum. Mol. Genet. , vol.13 , pp. 1183-1192
    • Minamiyama, M.1    Katsuno, M.2    Adachi, H.3    Waza, M.4    Sang, C.5    Kobayashi, Y.6
  • 80
    • 0030670816 scopus 로고    scopus 로고
    • Dentatorubral pallidoluysian atrophy (DRPLA) protein is cleaved by caspase-3 during apoptosis
    • Miyashita, T., Okamura-Oho, Y., Mito, Y., Nagafuchi, S., and Yamada, M. (1997). Dentatorubral pallidoluysian atrophy (DRPLA) protein is cleaved by caspase-3 during apoptosis. J. Biol. Chem. 272, 29238–29242. doi: 10.1074/jbc.272.46.29238
    • (1997) J. Biol. Chem. , vol.272 , pp. 29238-29242
    • Miyashita, T.1    Okamura-Oho, Y.2    Mito, Y.3    Nagafuchi, S.4    Yamada, M.5
  • 81
    • 82555200920 scopus 로고    scopus 로고
    • SIRT1 modulates aggregation and toxicity through deacetylation of the androgen receptor in cell models of SBMA
    • Montie, H. L., Pestell, R. G., and Merry, D. E. (2011). SIRT1 modulates aggregation and toxicity through deacetylation of the androgen receptor in cell models of SBMA. J. Neurosci. 31, 17425–17436. doi: 10.1523/JNEUROSCI.3958-11.2011
    • (2011) J. Neurosci. , vol.31 , pp. 17425-17436
    • Montie, H.L.1    Pestell, R.G.2    Merry, D.E.3
  • 82
    • 72849148037 scopus 로고    scopus 로고
    • Posttranslational modification of ataxin-7 at lysine 257 prevents autophagy-mediated turnover of an N-terminal caspase-7 cleavage fragment
    • Mookerjee, S., Papanikolaou, T., Guyenet, S. J., Sampath, V., Lin, A., Vitelli, C., et al. (2009). Posttranslational modification of ataxin-7 at lysine 257 prevents autophagy-mediated turnover of an N-terminal caspase-7 cleavage fragment. J. Neurosci. 29, 15134–15144. doi: 10.1523/JNEUROSCI.4720-09.2009
    • (2009) J. Neurosci. , vol.29 , pp. 15134-15144
    • Mookerjee, S.1    Papanikolaou, T.2    Guyenet, S.J.3    Sampath, V.4    Lin, A.5    Vitelli, C.6
  • 83
    • 68749103450 scopus 로고    scopus 로고
    • CK2-dependent phosphorylation determines cellular localization and stability of ataxin-3
    • Mueller, T., Breuer, P., Schmitt, I., Walter, J., Evert, B. O., and Wullner, U. (2009). CK2-dependent phosphorylation determines cellular localization and stability of ataxin-3. Hum. Mol. Genet. 18, 3334–3343. doi: 10.1093/hmg/ddp274
    • (2009) Hum. Mol. Genet. , vol.18 , pp. 3334-3343
    • Mueller, T.1    Breuer, P.2    Schmitt, I.3    Walter, J.4    Evert, B.O.5    Wullner, U.6
  • 84
    • 69249090927 scopus 로고    scopus 로고
    • Small ubiquitin-like modifier (SUMO) modification of the androgen receptor attenuates polyglutamine-mediated aggregation
    • Mukherjee, S., Thomas, M., Dadgar, N., Lieberman, A. P., and Iniguez-Lluhi, J. A. (2009). Small ubiquitin-like modifier (SUMO) modification of the androgen receptor attenuates polyglutamine-mediated aggregation. J. Biol. Chem. 284, 21296–21306. doi: 10.1074/jbc.M109.011494
    • (2009) J. Biol. Chem. , vol.284 , pp. 21296-21306
    • Mukherjee, S.1    Thomas, M.2    Dadgar, N.3    Lieberman, A.P.4    Iniguez-Lluhi, J.A.5
  • 85
    • 77957011660 scopus 로고    scopus 로고
    • Native functions of the androgen receptor are essential to pathogenesis in a Drosophila model of spinobulbar muscular atrophy
    • Nedelsky, N. B., Pennuto, M., Smith, R. B., Palazzolo, I., Moore, J., Nie, Z., et al. (2010). Native functions of the androgen receptor are essential to pathogenesis in a Drosophila model of spinobulbar muscular atrophy. Neuron 67, 936–952. doi: 10.1016/j.neuron.2010.08.034
    • (2010) Neuron , vol.67 , pp. 936-952
    • Nedelsky, N.B.1    Pennuto, M.2    Smith, R.B.3    Palazzolo, I.4    Moore, J.5    Nie, Z.6
  • 86
    • 59249085091 scopus 로고    scopus 로고
    • Phosphorylation of S409/410 of TDP-43 is a consistent feature in all sporadic and familial forms of TDP-43 proteinopathies
    • Neumann, M., Kwong, L. K., Lee, E. B., Kremmer, E., Flatley, A., Xu, Y., et al. (2009). Phosphorylation of S409/410 of TDP-43 is a consistent feature in all sporadic and familial forms of TDP-43 proteinopathies. Acta Neuropathol. 117, 137–149. doi: 10.1007/s00401-008-0477-9
    • (2009) Acta Neuropathol , vol.117 , pp. 137-149
    • Neumann, M.1    Kwong, L.K.2    Lee, E.B.3    Kremmer, E.4    Flatley, A.5    Xu, Y.6
  • 87
    • 33749632259 scopus 로고    scopus 로고
    • Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis
    • Neumann, M., Sampathu, D. M., Kwong, L. K., Truax, A. C., Micsenyi, M. C., Chou, T. T., et al. (2006). Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis. Science 314, 130–133. doi: 10.1126/science.1134108
    • (2006) Science , vol.314 , pp. 130-133
    • Neumann, M.1    Sampathu, D.M.2    Kwong, L.K.3    Truax, A.C.4    Micsenyi, M.C.5    Chou, T.T.6
  • 88
    • 84903398744 scopus 로고    scopus 로고
    • SUMO3 modification accelerates the aggregation of ALS-linked SOD1 mutants
    • Niikura, T., Kita, Y., and Abe, Y. (2014). SUMO3 modification accelerates the aggregation of ALS-linked SOD1 mutants. PLoS ONE 9:e101080. doi: 10.1371/journal.pone.0101080
    • (2014) Plos ONE , vol.9
    • Niikura, T.1    Kita, Y.2    Abe, Y.3
  • 89
    • 0035937523 scopus 로고    scopus 로고
    • Interference by huntingtin and atrophin-1 with cbp-mediated transcription leading to cellular toxicity
    • Nucifora, F. C. Jr., Sasaki, M., Peters, M. F., Huang, H., Cooper, J. K., Yamada, M., et al. (2001). Interference by huntingtin and atrophin-1 with cbp-mediated transcription leading to cellular toxicity. Science 291, 2423–2428. doi: 10.1126/science.1056784
    • (2001) Science , vol.291 , pp. 2423-2428
    • Nucifora, F.C.1    Sasaki, M.2    Peters, M.F.3    Huang, H.4    Cooper, J.K.5    Yamada, M.6
  • 90
    • 0033587128 scopus 로고    scopus 로고
    • Inhibition of caspase-1 slows disease progression in a mouse model of Huntington’s disease
    • Ona, V. O., Li, M., Vonsattel, J. P., Andrews, L. J., Khan, S. Q., Chung, W. M., et al. (1999). Inhibition of caspase-1 slows disease progression in a mouse model of Huntington’s disease. Nature 399, 263–267. doi: 10.1038/20446
    • (1999) Nature , vol.399 , pp. 263-267
    • Ona, V.O.1    Li, M.2    Vonsattel, J.P.3    Andrews, L.J.4    Khan, S.Q.5    Chung, W.M.6
  • 91
    • 34547692622 scopus 로고    scopus 로고
    • Trinucleotide repeat disorders
    • Orr, H. T., and Zoghbi, H. Y. (2007). Trinucleotide repeat disorders. Annu. Rev. Neurosci. 30, 575–621. doi: 10.1146/annurev.neuro.29.051605.113042
    • (2007) Annu. Rev. Neurosci. , vol.30 , pp. 575-621
    • Orr, H.T.1    Zoghbi, H.Y.2
  • 92
    • 34447309577 scopus 로고    scopus 로고
    • Akt blocks ligand binding and protects against expanded polyglutamine androgen receptor toxicity
    • Palazzolo, I., Burnett, B. G., Young, J. E., Brenne, P. L., La Spada, A. R., Fischbeck, K. H., et al. (2007). Akt blocks ligand binding and protects against expanded polyglutamine androgen receptor toxicity. Hum. Mol. Genet. 16, 1593–1603. doi: 10.1093/hmg/ddm109
    • (2007) Hum. Mol. Genet. , vol.16 , pp. 1593-1603
    • Palazzolo, I.1    Burnett, B.G.2    Young, J.E.3    Brenne, P.L.4    La Spada, A.R.5    Fischbeck, K.H.6
  • 93
    • 77953648932 scopus 로고    scopus 로고
    • B2 attenuates polyglutamine-expanded androgen receptor toxicity in cell and fly models of spinal and bulbar muscular atrophy
    • Palazzolo, I., Nedelsky, N. B., Askew, C. E., Harmison, G. G., Kasantsev, A. G., Taylor, J. P., et al. (2010). B2 attenuates polyglutamine-expanded androgen receptor toxicity in cell and fly models of spinal and bulbar muscular atrophy. J. Neurosci. Res. 88, 2207–2216. doi: 10.1002/jnr.22389
    • (2010) J. Neurosci. Res. , vol.88 , pp. 2207-2216
    • Palazzolo, I.1    Nedelsky, N.B.2    Askew, C.E.3    Harmison, G.G.4    Kasantsev, A.G.5    Taylor, J.P.6
  • 94
    • 68149180778 scopus 로고    scopus 로고
    • Overexpression of IGF-1 in muscle attenuates disease in a mouse model of spinal and bulbar muscular atrophy
    • Palazzolo, I., Stack, C., Kong, L., Musaro, A., Adachi, H., Katsuno, M., et al. (2009). Overexpression of IGF-1 in muscle attenuates disease in a mouse model of spinal and bulbar muscular atrophy. Neuron 63, 316–328. doi: 10.1016/j.neuron.2009.07.019
    • (2009) Neuron , vol.63 , pp. 316-328
    • Palazzolo, I.1    Stack, C.2    Kong, L.3    Musaro, A.4    Adachi, H.5    Katsuno, M.6
  • 95
    • 32544432052 scopus 로고    scopus 로고
    • Inhibition of calcineurin by FK506 protects against polyglutamine-huntingtin toxicity through an increase of huntingtin phosphorylation at S421
    • Pardo, R., Colin, E., Regulier, E., Aebischer, P., Deglon, N., Humbert, S., et al. (2006). Inhibition of calcineurin by FK506 protects against polyglutamine-huntingtin toxicity through an increase of huntingtin phosphorylation at S421. J. Neurosci. 26, 1635–1645. doi: 10.1523/JNEUROSCI.3706-05.2006
    • (2006) J. Neurosci. , vol.26 , pp. 1635-1645
    • Pardo, R.1    Colin, E.2    Regulier, E.3    Aebischer, P.4    Deglon, N.5    Humbert, S.6
  • 96
    • 84879414055 scopus 로고    scopus 로고
    • RAS-MAPK-MSK1 pathway modulates ataxin 1 protein levels and toxicity in SCA1
    • Park, J., Al-Ramahi, I., Tan, Q., Mollema, N., Diaz-Garcia, J. R., Gallego-Flores, T., et al. (2013). RAS-MAPK-MSK1 pathway modulates ataxin 1 protein levels and toxicity in SCA1. Nature 498, 325–331. doi: 10.1038/nature12204
    • (2013) Nature , vol.498 , pp. 325-331
    • Park, J.1    Al-Ramahi, I.2    Tan, Q.3    Mollema, N.4    Diaz-Garcia, J.R.5    Gallego-Flores, T.6
  • 98
    • 85007018158 scopus 로고    scopus 로고
    • Adenylyl cyclase activating polypeptide reduces phosphorylation and toxicity of the polyglutamine-expanded androgen receptor in spinobulbar muscular atrophy
    • Polanco, M. J., Parodi, S., Piol, D., Stack, C., Chivet, M., Contestabile, A., et al. (2016). Adenylyl cyclase activating polypeptide reduces phosphorylation and toxicity of the polyglutamine-expanded androgen receptor in spinobulbar muscular atrophy. Sci. Transl. Med. 8, 370ra181. doi: 10.1126/scitranslmed.aaf9526
    • (2016) Sci. Transl. Med. , vol.8
    • Polanco, M.J.1    Parodi, S.2    Piol, D.3    Stack, C.4    Chivet, M.5    Contestabile, A.6
  • 99
    • 0034687807 scopus 로고    scopus 로고
    • Covalent modification of the androgen receptor by small ubiquitin-like modifier 1 (SUMO-1
    • Poukka, H., Karvonen, U., Janne, O. A., and Palvimo, J. J. (2000). Covalent modification of the androgen receptor by small ubiquitin-like modifier 1 (SUMO-1). Proc. Natl. Acad. Sci. U.S.A. 97, 14145–14150. doi: 10.1073/pnas. 97.26.14145
    • (2000) Proc. Natl. Acad. Sci. U.S.A , vol.97 , pp. 14145-14150
    • Poukka, H.1    Karvonen, U.2    Janne, O.A.3    Palvimo, J.J.4
  • 100
    • 0842265636 scopus 로고    scopus 로고
    • The serum- and glucocorticoid-induced kinase SGK inhibits mutant huntingtin-induced toxicity by phosphorylating serine 421 of huntingtin
    • Rangone, H., Poizat, G., Troncoso, J., Ross, C. A., MacDonald, M. E., Saudou, F., et al. (2004). The serum- and glucocorticoid-induced kinase SGK inhibits mutant huntingtin-induced toxicity by phosphorylating serine 421 of huntingtin. Eur. J. Neurosci. 19, 273–279. doi: 10.1111/j.0953-816X. 2003.03131.x
    • (2004) Eur. J. Neurosci. , vol.19 , pp. 273-279
    • Rangone, H.1    Poizat, G.2    Troncoso, J.3    Ross, C.A.4    Macdonald, M.E.5    Saudou, F.6
  • 101
    • 0038000050 scopus 로고    scopus 로고
    • Detection of arginine dimethylated peptides by parallel precursor ion scanning mass spectrometry in positive ion mode
    • Rappsilber, J., Friesen, W. J., Paushkin, S., Dreyfuss, G., and Mann, M. (2003). Detection of arginine dimethylated peptides by parallel precursor ion scanning mass spectrometry in positive ion mode. Anal. Chem. 75, 3107–3114. doi: 10.1021/ac026283q
    • (2003) Anal. Chem. , vol.75 , pp. 3107-3114
    • Rappsilber, J.1    Friesen, W.J.2    Paushkin, S.3    Dreyfuss, G.4    Mann, M.5
  • 102
    • 84929635972 scopus 로고    scopus 로고
    • PRMT5- mediated symmetric arginine dimethylation is attenuated by mutant huntingtin and is impaired in Huntington’s disease (HD)
    • Ratovitski, T., Arbez, N., Stewart, J. C., Chighladze, E., and Ross, C. A. (2015). PRMT5- mediated symmetric arginine dimethylation is attenuated by mutant huntingtin and is impaired in Huntington’s disease (HD). Cell Cycle 14, 1716–1729. doi: 10.1080/15384101.2015.1033595
    • (2015) Cell Cycle , vol.14 , pp. 1716-1729
    • Ratovitski, T.1    Arbez, N.2    Stewart, J.C.3    Chighladze, E.4    Ross, C.A.5
  • 103
    • 20444467297 scopus 로고    scopus 로고
    • SUMOylation of the polyglutamine repeat protein, ataxin-1, is dependent on a functional nuclear localization signal
    • Riley, B. E., Zoghbi, H. Y., and Orr, H. T. (2005). SUMOylation of the polyglutamine repeat protein, ataxin-1, is dependent on a functional nuclear localization signal. J. Biol. Chem. 280, 21942–21948. doi: 10.1074/jbc.M501677200
    • (2005) J. Biol. Chem. , vol.280 , pp. 21942-21948
    • Riley, B.E.1    Zoghbi, H.Y.2    Orr, H.T.3
  • 104
    • 84869127465 scopus 로고    scopus 로고
    • Insulinlike Growth Factor (IGF)-1 administration ameliorates disease manifestations in a mouse model of spinal and bulbar muscular atrophy
    • Rinaldi, C., Bott, L. C., Chen, K. L., Harmison, G. G., Katsuno, M., Sobue, G., et al. (2012). Insulinlike Growth Factor (IGF)-1 administration ameliorates disease manifestations in a mouse model of spinal and bulbar muscular atrophy. Mol. Med. 18, 1261–1268. doi: 10.2119/molmed.2012.00271
    • (2012) Mol. Med , vol.18 , pp. 1261-1268
    • Rinaldi, C.1    Bott, L.C.2    Chen, K.L.3    Harmison, G.G.4    Katsuno, M.5    Sobue, G.6
  • 105
    • 84960446275 scopus 로고    scopus 로고
    • Glycolytic-to-oxidative fiber-type switch and mTOR signaling activation are early-onset features of SBMA muscle modified by high-fat diet
    • Rocchi, A., Milioto, C., Parodi, S., Armirotti, A., Borgia, D., Pellegrini, M., et al. (2016). Glycolytic-to-oxidative fiber-type switch and mTOR signaling activation are early-onset features of SBMA muscle modified by high-fat diet. Acta Neuropathol. 132, 127–144. doi: 10.1007/s00401-016-1550-4
    • (2016) Acta Neuropathol , vol.132 , pp. 127-144
    • Rocchi, A.1    Milioto, C.2    Parodi, S.3    Armirotti, A.4    Borgia, D.5    Pellegrini, M.6
  • 106
    • 77649184659 scopus 로고    scopus 로고
    • Oxidative stress-enhanced SUMOylation and aggregation of ataxin-1: Implication of JNK pathway
    • Ryu, J., Cho, S., Park, B. C., and Lee, D. H. (2010). Oxidative stress-enhanced SUMOylation and aggregation of ataxin-1: implication of JNK pathway. Biochem. Biophys. Res. Commun. 393, 280–285. doi: 10.1016/j.bbrc.2010. 01.122
    • (2010) Biochem. Biophys. Res. Commun. , vol.393 , pp. 280-285
    • Ryu, J.1    Cho, S.2    Park, B.C.3    Lee, D.H.4
  • 107
    • 0033103523 scopus 로고    scopus 로고
    • Caspase-8 is required for cell death induced by expanded polyglutamine repeats
    • Sanchez, I., Xu, C. J., Juo, P., Kakizaka, A., Blenis, J., and Yuan, J. (1999). Caspase-8 is required for cell death induced by expanded polyglutamine repeats. Neuron 22, 623–633. doi: 10.1016/S0896-6273(00)80716-3
    • (1999) Neuron , vol.22 , pp. 623-633
    • Sanchez, I.1    Xu, C.J.2    Juo, P.3    Kakizaka, A.4    Blenis, J.5    Yuan, J.6
  • 108
    • 84920749607 scopus 로고    scopus 로고
    • Protein arginine methyltransferase 6 enhances polyglutamine-expanded androgen receptor function and toxicity in spinal and bulbar muscular atrophy
    • Scaramuzzino, C., Casci, I., Parodi, S., Lievens, P. M., Polanco, M. J., Milioto, C., et al. (2015). Protein arginine methyltransferase 6 enhances polyglutamine-expanded androgen receptor function and toxicity in spinal and bulbar muscular atrophy. Neuron 85, 88–100. doi: 10.1016/j.neuron.2014.12.031
    • (2015) Neuron , vol.85 , pp. 88-100
    • Scaramuzzino, C.1    Casci, I.2    Parodi, S.3    Lievens, P.M.4    Polanco, M.J.5    Milioto, C.6
  • 109
    • 84876437828 scopus 로고    scopus 로고
    • Protein arginine methyltransferase 1 and 8 interact with FUS to modify its sub-cellular distribution and toxicity in vitro and in vivo
    • Scaramuzzino, C., Monaghan, J., Milioto, C., Lanson, N. A. Jr., Maltare, A., Aggarwal, T., et al. (2013). Protein arginine methyltransferase 1 and 8 interact with FUS to modify its sub-cellular distribution and toxicity in vitro and in vivo. PLoS ONE 8:e61576. doi: 10.1371/journal.pone.0061576
    • (2013) Plos ONE , vol.8
    • Scaramuzzino, C.1    Monaghan, J.2    Milioto, C.3    Lanson, N.A.4    Maltare, A.5    Aggarwal, T.6
  • 110
    • 33747633422 scopus 로고    scopus 로고
    • Huntingtin phosphorylation sites mapped by mass spectrometry. Modulation of cleavage and toxicity
    • Schilling, B., Gafni, J., Torcassi, C., Cong, X., Row, R. H., LaFevre-Bernt, M. A., et al. (2006). Huntingtin phosphorylation sites mapped by mass spectrometry. Modulation of cleavage and toxicity. J. Biol. Chem. 281, 23686–23697. doi: 10.1074/jbc.M513507200
    • (2006) J. Biol. Chem. , vol.281 , pp. 23686-23697
    • Schilling, B.1    Gafni, J.2    Torcassi, C.3    Cong, X.4    Row, R.H.5    Lafevre-Bernt, M.A.6
  • 111
    • 77950658888 scopus 로고    scopus 로고
    • Multiplex SILAC analysis of a cellular TDP-43 proteinopathy model reveals protein inclusions associated with SUMOylation and diverse polyubiquitin chains
    • Seyfried, N. T., Gozal, Y. M., Dammer, E. B., Xia, Q., Duong, D. M., Cheng, D., et al. (2010). Multiplex SILAC analysis of a cellular TDP-43 proteinopathy model reveals protein inclusions associated with SUMOylation and diverse polyubiquitin chains. Mol. Cell. Proteomics 9, 705–718. doi: 10.1074/mcp.M800390-MCP200
    • (2010) Mol. Cell. Proteomics , vol.9 , pp. 705-718
    • Seyfried, N.T.1    Gozal, Y.M.2    Dammer, E.B.3    Xia, Q.4    Duong, D.M.5    Cheng, D.6
  • 112
    • 50249147874 scopus 로고    scopus 로고
    • Phosphorylation of profilin by ROCK1 regulates polyglutamine aggregation
    • Shao, J., Welch, W. J., Diprospero, N. A., and Diamond, M. I. (2008). Phosphorylation of profilin by ROCK1 regulates polyglutamine aggregation. Mol. Cell. Biol. 28, 5196–5208. doi: 10.1128/MCB.00079-08
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 5196-5208
    • Shao, J.1    Welch, W.J.2    Diprospero, N.A.3    Diamond, M.I.4
  • 113
    • 11144353613 scopus 로고    scopus 로고
    • SUMOmodification of Huntingtin and Huntington’s disease pathology
    • Steffan, J. S., Agrawal, N., Pallos, J., Rockabrand, E., Trotman, L. C., Slepko, N., et al. (2004). SUMOmodification of Huntingtin and Huntington’s disease pathology. Science 304, 100–104. doi: 10.1126/science.1092194
    • (2004) Science , vol.304 , pp. 100-104
    • Steffan, J.S.1    Agrawal, N.2    Pallos, J.3    Rockabrand, E.4    Trotman, L.C.5    Slepko, N.6
  • 114
    • 84961231197 scopus 로고    scopus 로고
    • Monomethylated and unmethylated FUS exhibit increased binding to Transportin and distinguish FTLD-FUS from ALS-FUS
    • Suarez-Calvet, M., Neumann, M., Arzberger, T., Abou-Ajram, C., Funk, E., Hartmann, H., et al. (2016). Monomethylated and unmethylated FUS exhibit increased binding to Transportin and distinguish FTLD-FUS from ALS-FUS. Acta Neuropathol. 131, 587–604. doi: 10.1007/s00401-016-1544-2
    • (2016) Acta Neuropathol , vol.131 , pp. 587-604
    • Suarez-Calvet, M.1    Neumann, M.2    Arzberger, T.3    Abou-Ajram, C.4    Funk, E.5    Hartmann, H.6
  • 115
    • 53949117951 scopus 로고    scopus 로고
    • Casein kinase 2 interacts with and phosphorylates ataxin-3
    • Tao, R. S., Fei, E. K., Ying, Z., Wang, H. F., and Wang, G. H. (2008). Casein kinase 2 interacts with and phosphorylates ataxin-3. Neurosci. Bull. 24, 271–277. doi: 10.1007/s12264-008-0605-5
    • (2008) Neurosci. Bull. , vol.24 , pp. 271-277
    • Tao, R.S.1    Fei, E.K.2    Ying, Z.3    Wang, H.F.4    Wang, G.H.5
  • 116
    • 85012041135 scopus 로고    scopus 로고
    • Decoding ALS: From genes to mechanism
    • Taylor, J. P., Brown, R. H. Jr., and Cleveland, D. W. (2016). Decoding ALS: from genes to mechanism. Nature 539, 197–206. doi: 10.1038/nature20413
    • (2016) Nature , vol.539 , pp. 197-206
    • Taylor, J.P.1    Brown, R.H.2    Cleveland, D.W.3
  • 117
    • 0038722748 scopus 로고    scopus 로고
    • Aberrant histone acetylation, altered transcription, and retinal degeneration in a Drosophila model of polyglutamine disease are rescued by CREB-binding protein
    • Taylor, J. P., Taye, A. A., Campbell, C., Kazemi-Esfarjani, P., Fischbeck, K. H., and Min, K. T. (2003). Aberrant histone acetylation, altered transcription, and retinal degeneration in a Drosophila model of polyglutamine disease are rescued by CREB-binding protein. Genes Dev. 17, 1463–1468. doi: 10.1101/gad.1087503
    • (2003) Genes Dev , vol.17 , pp. 1463-1468
    • Taylor, J.P.1    Taye, A.A.2    Campbell, C.3    Kazemi-Esfarjani, P.4    Fischbeck, K.H.5    Min, K.T.6
  • 118
    • 0037015833 scopus 로고    scopus 로고
    • SUMO-1 co-localized with mutant atrophin-1 with expanded polyglutamines accelerates intranuclear aggregation and cell death
    • Terashima, T., Kawai, H., Fujitani, M., Maeda, K., and Yasuda, H. (2002). SUMO-1 co-localized with mutant atrophin-1 with expanded polyglutamines accelerates intranuclear aggregation and cell death. Neuroreport 13, 2359–2364. doi: 10.1097/00001756-200212030-00038
    • (2002) Neuroreport , vol.13 , pp. 2359-2364
    • Terashima, T.1    Kawai, H.2    Fujitani, M.3    Maeda, K.4    Yasuda, H.5
  • 119
    • 72149124383 scopus 로고    scopus 로고
    • IKK phosphorylates Huntingtin and targets it for degradation by the proteasome and lysosome
    • Thompson, L. M., Aiken, C. T., Kaltenbach, L. S., Agrawal, N., Illes, K., Khoshnan, A., et al. (2009). IKK phosphorylates Huntingtin and targets it for degradation by the proteasome and lysosome. J. Cell Biol. 187, 1083–1099. doi: 10.1083/jcb.200909067
    • (2009) J. Cell Biol. , vol.187 , pp. 1083-1099
    • Thompson, L.M.1    Aiken, C.T.2    Kaltenbach, L.S.3    Agrawal, N.4    Illes, K.5    Khoshnan, A.6
  • 120
    • 84922423167 scopus 로고    scopus 로고
    • Cytoplasmic sequestration of FUS/TLS associated with ALS alters histone marks through loss of nuclear protein arginine methyltransferase 1
    • Tibshirani, M., Tradewell, M. L., Mattina, K. R., Minotti, S., Yang, W., Zhou, H., et al. (2015). Cytoplasmic sequestration of FUS/TLS associated with ALS alters histone marks through loss of nuclear protein arginine methyltransferase 1. Hum. Mol. Genet. 24, 773–786. doi: 10.1093/hmg/ddu494
    • (2015) Hum. Mol. Genet. , vol.24 , pp. 773-786
    • Tibshirani, M.1    Tradewell, M.L.2    Mattina, K.R.3    Minotti, S.4    Yang, W.5    Zhou, H.6
  • 121
    • 83455162720 scopus 로고    scopus 로고
    • Arginine methylation by PRMT1 regulates nuclear-cytoplasmic localization and toxicity of FUS/TLS harbouring ALS-linked mutations
    • Tradewell, M. L., Yu, Z., Tibshirani, M., Boulanger, M. C., Durham, H. D., and Richard, S. (2012). Arginine methylation by PRMT1 regulates nuclear-cytoplasmic localization and toxicity of FUS/TLS harbouring ALS-linked mutations. Hum. Mol. Genet. 21, 136–149. doi: 10.1093/hmg/ddr448
    • (2012) Hum. Mol. Genet. , vol.21 , pp. 136-149
    • Tradewell, M.L.1    Yu, Z.2    Tibshirani, M.3    Boulanger, M.C.4    Durham, H.D.5    Richard, S.6
  • 122
    • 0038159253 scopus 로고    scopus 로고
    • Parkin facilitates the elimination of expanded polyglutamine proteins and leads to preservation of proteasome function
    • Tsai, Y. C., Fishman, P. S., Thakor, N. V., and Oyler, G. A. (2003). Parkin facilitates the elimination of expanded polyglutamine proteins and leads to preservation of proteasome function. J. Biol. Chem. 278, 22044–22055. doi: 10.1074/jbc.M212235200
    • (2003) J. Biol. Chem. , vol.278 , pp. 22044-22055
    • Tsai, Y.C.1    Fishman, P.S.2    Thakor, N.V.3    Oyler, G.A.4
  • 123
    • 84976867081 scopus 로고    scopus 로고
    • Pathogenic mutations in the valosin-containing Protein/p97(VCP) N-domain inhibit the SUMOylation of VCP and Lead to impaired stress response
    • Wang, T., Xu, W., Qin, M., Yang, Y., Bao, P., Shen, F., et al. (2016). Pathogenic mutations in the valosin-containing Protein/p97(VCP) N-domain inhibit the SUMOylation of VCP and Lead to impaired stress response. J. Biol. Chem. 291, 14373–14384. doi: 10.1074/jbc.M116.729343
    • (2016) J. Biol. Chem. , vol.291 , pp. 14373-14384
    • Wang, T.1    Xu, W.2    Qin, M.3    Yang, Y.4    Bao, P.5    Shen, F.6
  • 124
    • 20444448900 scopus 로고    scopus 로고
    • Huntingtin phosphorylation on serine 421 is significantly reduced in the striatum and by polyglutamine expansion in vivo
    • Warby, S. C., Chan, E. Y., Metzler, M., Gan, L., Singaraja, R. R., Crocker, S. F., et al. (2005). Huntingtin phosphorylation on serine 421 is significantly reduced in the striatum and by polyglutamine expansion in vivo. Hum. Mol. Genet. 14, 1569–1577. doi: 10.1093/hmg/ddi165
    • (2005) Hum. Mol. Genet. , vol.14 , pp. 1569-1577
    • Warby, S.C.1    Chan, E.Y.2    Metzler, M.3    Gan, L.4    Singaraja, R.R.5    Crocker, S.F.6
  • 125
    • 15944419824 scopus 로고    scopus 로고
    • Ataxin-3 suppresses polyglutamine neurodegeneration in Drosophila by a ubiquitin-associated mechanism
    • Warrick, J. M., Morabito, L. M., Bilen, J., Gordesky-Gold, B., Faust, L. Z., Paulson, H. L., et al. (2005). Ataxin-3 suppresses polyglutamine neurodegeneration in Drosophila by a ubiquitin-associated mechanism. Mol. Cell 18, 37–48. doi: 10.1016/j.molcel.2005.02.030
    • (2005) Mol. Cell , vol.18 , pp. 37-48
    • Warrick, J.M.1    Morabito, L.M.2    Bilen, J.3    Gordesky-Gold, B.4    Faust, L.Z.5    Paulson, H.L.6
  • 126
    • 0032502715 scopus 로고    scopus 로고
    • Caspase cleavage of gene products associated with triplet expansion disorders generates truncated fragments containing the polyglutamine tract
    • Wellington, C. L., Ellerby, L. M., Hackam, A. S., Margolis, R. L., Trifiro, M. A., Singaraja, R., et al. (1998). Caspase cleavage of gene products associated with triplet expansion disorders generates truncated fragments containing the polyglutamine tract. J. Biol. Chem. 273, 9158–9167. doi: 10.1074/jbc. 273.15.9158
    • (1998) J. Biol. Chem , vol.273 , pp. 9158-9167
    • Wellington, C.L.1    Ellerby, L.M.2    Hackam, A.S.3    Margolis, R.L.4    Trifiro, M.A.5    Singaraja, R.6
  • 127
    • 0034733607 scopus 로고    scopus 로고
    • Inhibiting caspase cleavage of huntingtin reduces toxicity and aggregate formation in neuronal and nonneuronal cells
    • Wellington, C. L., Singaraja, R., Ellerby, L., Savill, J., Roy, S., Leavitt, B., et al. (2000). Inhibiting caspase cleavage of huntingtin reduces toxicity and aggregate formation in neuronal and nonneuronal cells. J. Biol. Chem. 275, 19831–19838. doi: 10.1074/jbc.M001475200
    • (2000) J. Biol. Chem. , vol.275 , pp. 19831-19838
    • Wellington, C.L.1    Singaraja, R.2    Ellerby, L.3    Savill, J.4    Roy, S.5    Leavitt, B.6
  • 128
    • 33745627659 scopus 로고    scopus 로고
    • Palmitoylation of huntingtin by HIP14 is essential for its trafficking and function
    • Yanai, A., Huang, K., Kang, R., Singaraja, R. R., Arstikaitis, P., Gan, L., et al. (2006). Palmitoylation of huntingtin by HIP14 is essential for its trafficking and function. Nat. Neurosci. 9, 824–831. doi: 10.1038/nn1702
    • (2006) Nat. Neurosci. , vol.9 , pp. 824-831
    • Yanai, A.1    Huang, K.2    Kang, R.3    Singaraja, R.R.4    Arstikaitis, P.5    Gan, L.6
  • 129
    • 33744965475 scopus 로고    scopus 로고
    • Sodium butyrate ameliorates histone hypoacetylation and neurodegenerative phenotypes in a mouse model for DRPLA
    • Ying, M., Xu, R., Wu, X., Zhu, H., Zhuang, Y., Han, M., et al. (2006). Sodium butyrate ameliorates histone hypoacetylation and neurodegenerative phenotypes in a mouse model for DRPLA. J. Biol. Chem. 281, 12580–12586. doi: 10.1074/jbc.M511677200
    • (2006) J. Biol. Chem. , vol.281 , pp. 12580-12586
    • Ying, M.1    Xu, R.2    Wu, X.3    Zhu, H.4    Zhuang, Y.5    Han, M.6
  • 130
    • 35648964788 scopus 로고    scopus 로고
    • Proteolytic cleavage of ataxin-7 by caspase-7 modulates cellular toxicity and transcriptional dysregulation
    • Young, J. E., Gouw, L., Propp, S., Sopher, B. L., Taylor, J., Lin, A., et al. (2007). Proteolytic cleavage of ataxin-7 by caspase-7 modulates cellular toxicity and transcriptional dysregulation. J. Biol. Chem. 282, 30150–30160. doi: 10.1074/jbc.M705265200
    • (2007) J. Biol. Chem. , vol.282 , pp. 30150-30160
    • Young, J.E.1    Gouw, L.2    Propp, S.3    Sopher, B.L.4    Taylor, J.5    Lin, A.6
  • 131
    • 84946222547 scopus 로고    scopus 로고
    • Blocking the association of HDAC4 with MAP1S accelerates autophagy clearance of mutant Huntingtin
    • Yue, F., Li, W., Zou, J., Chen, Q., Xu, G., Huang, H., et al. (2015). Blocking the association of HDAC4 with MAP1S accelerates autophagy clearance of mutant Huntingtin. Aging 7, 839–853. doi: 10.18632/aging. 100818
    • (2015) Aging , vol.7 , pp. 839-853
    • Yue, F.1    Li, W.2    Zou, J.3    Chen, Q.4    Xu, G.5    Huang, H.6
  • 132
    • 85040709233 scopus 로고    scopus 로고
    • Phosphorylation regulates proteasomal-mediated degradation and solubility of TAR DNA binding protein-43 C-terminal fragments
    • Zhang, Y. J., Gendron, T. F., Xu, Y. F., Ko, L. W., Yen, S. H., and Petrucelli, L. (2010). Phosphorylation regulates proteasomal-mediated degradation and solubility of TAR DNA binding protein-43 C-terminal fragments. Mol. Neurodegener. 5:33. doi: 10.1186/1750-1326-5-33
    • (2010) Mol. Neurodegener. , vol.5 , pp. 33
    • Zhang, Y.J.1    Gendron, T.F.2    Xu, Y.F.3    Ko, L.W.4    Yen, S.H.5    Petrucelli, L.6
  • 133
    • 66149114101 scopus 로고    scopus 로고
    • Aberrant cleavage of TDP-43 enhances aggregation and cellular toxicity
    • Zhang, Y. J., Xu, Y. F., Cook, C., Gendron, T. F., Roettges, P., Link, C. D., et al. (2009). Aberrant cleavage of TDP-43 enhances aggregation and cellular toxicity. Proc. Natl. Acad. Sci. U.S.A. 106, 7607–7612. doi: 10.1073/pnas.09006 88106
    • (2009) Proc. Natl. Acad. Sci. U.S.A , vol.106 , pp. 7607-7612
    • Zhang, Y.J.1    Xu, Y.F.2    Cook, C.3    Gendron, T.F.4    Roettges, P.5    Link, C.D.6
  • 134
    • 34848921202 scopus 로고    scopus 로고
    • Progranulin mediates caspase-dependent cleavage of TAR DNA binding protein-43
    • Zhang, Y. J., Xu, Y. F., Dickey, C. A., Buratti, E., Baralle, F., Bailey, R., et al. (2007). Progranulin mediates caspase-dependent cleavage of TAR DNA binding protein-43. J. Neurosci. 27, 10530–10534. doi: 10.1523/JNEUROSCI.3421-07.2007
    • (2007) J. Neurosci. , vol.27 , pp. 10530-10534
    • Zhang, Y.J.1    Xu, Y.F.2    Dickey, C.A.3    Buratti, E.4    Baralle, F.5    Bailey, R.6
  • 135
    • 84873176209 scopus 로고    scopus 로고
    • SUMO-1 modification on K166 of polyQ-expanded ataxin-3 strengthens its stability and increases its cytotoxicity
    • Zhou, Y. F., Liao, S. S., Luo, Y. Y., Tang, J. G., Wang, J. L., Lei, L. F., et al. (2013). SUMO-1 modification on K166 of polyQ-expanded ataxin-3 strengthens its stability and increases its cytotoxicity. PLoS ONE 8:e54214. doi: 10.1371/journal.pone.0054214
    • (2013) Plos ONE , vol.8
    • Zhou, Y.F.1    Liao, S.S.2    Luo, Y.Y.3    Tang, J.G.4    Wang, J.L.5    Lei, L.F.6


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