References
- Ross CA, Tabrizi SJ. Huntington’s disease: from molecular pathogenesis to clinical treatment. The Lancet Neurol. 2011;10:83–98.
- Cattaneo E. Dysfunction of wild-type huntingtin in Huntington disease. News Physiol Sci. 2003;18:34–37.
- Drouet V, Perrin V, Hassig R, et al. Sustained effects of nonallele-specific Huntingtin silencing. Ann Neurol. 2009;65:276–285.
- Boudreau RL, McBride JL, Martins I, et al. Nonallele-specific silencing of mutant and wild-type huntingtin demonstrates therapeutic efficacy in Huntington’s disease mice. Mol Ther. 2009;17:1053–1063.
- Auerbach W, Hurlbert MS, Hilditch-Maguire P, et al. The HD mutation causes progressive lethal neurological disease in mice expressing reduced levels of huntingtin. Hum Mol Genet. 2001;10:2515–2523.
- Walker FO. Huntington’s disease. Lancet. 2007;369:218–228.
- Vonsattel JP. Huntington disease models and human neuropathology: similarities and differences. Acta Neuropathol. 2008;115:55–69.
- Truant R, Atwal RS, Desmond C, Munsie L, Tran T. Huntington’s disease: revisiting the aggregation hypothesis in polyglutamine neurodegenerative diseases. FEBS J. 2008;275:4252–4262.
- Lu B, Palacino J. A novel human embryonic stem cell-derived Huntington’s disease neuronal model exhibits mutant huntingtin (mHTT) aggregates and soluble mHTT-dependent neurodegeneration. FASEB J. 2013;27:1820–1829.
- Cattaneo E, Zuccato C, Tartari M. Normal huntingtin function: an alternative approach to Huntington’s disease. Nat Rev Neurosci. 2005;6:919–930.
- Kim S, Kim KT. Therapeutic approaches for inhibition of protein aggregation in Huntington’s disease. Exp Neurobiol. 2014;23:36–44.
- Johri A, Chandra A, Beal MF. PGC-1α, mitochondrial dysfunction, and Huntington’s disease. Free Radic Biol Med. 2013;62:37–46.
- Sorolla MA, Reverter-Branchat G, Tamarit J, Ferrer I, Ros J, Cabiscol E. Proteomic and oxidative stress analysis in human brain samples of Huntington disease. Free Radic Biol Med. 2008;45:667–678.
- Wang JQ, Chen Q, Wang X, et al. Dysregulation of mitochondrial calcium signaling and superoxide flashes cause mitochondrial genomic DNA damage in Huntington disease. J Biol Chem. 2013;288:3070–3084.
- Martin DD, Ladha S, Ehrnhoefer DE, Hayden MR. Autophagy in Huntington disease and huntingtin in autophagy. Trends Neurosci. 2015;38:26–35.
- Gauthier LR, Charrin BC, Borrell-Pagès M, et al. Huntingtin controls neurotrophic support and survival of neurons by enhancing BDNF vesicular transport along microtubules. Cell. 2004;118:127–138.
- Dompierre JP, Godin JD, Charrin BC, et al. Histone deacetylase 6 inhibition compensates for the transport deficit in Huntington’s disease by increasing tubulin acetylation. J Neurosci. 2007;27:3571–3583.
- Yu S, Liang Y, Palacino J, Difiglia M, Lu B. Drugging unconventional targets: insights from Huntington’s disease. Trends Pharmacol Sci. 2014;35:53–62.
- Bjørkøy G, Lamark T, Brech A, et al. p62/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtin-induced cell death. J Cell Biol. 2005;171:603–614.
- Lu B, Al-Ramahi I, Valencia A, et al. Identification of NUB1 as a suppressor of mutant Huntington toxicity via enhanced protein clearance. Nat Neurosci. 2013;16:562–570.
- Ravikumar B, Vacher C, Berger Z, et al. Inhibition of mTOR induces autophagy and reduces toxicity of polyglutamine expansions in fly and mouse models of Huntington disease. Nat Genet. 2004;36:585–595.
- Sarkar S, Ravikumar B, Floto RA, Rubinsztein DC. Rapamycin and mTOR-independent autophagy inducers ameliorate toxicity of polyglutamine-expanded huntingtin and related proteinopathies. Cell Death Differ. 2009;16:46–56.
- Kito K, Yeh ET, Kamitani T. NUB1, a NEDD8-interacting protein, is induced by interferon and down-regulates the NEDD8 expression. J Biol Chem. 2001;276:20603–20609.
- Tanaka T, Kawashima H, Yeh ET, Kamitani T. Regulation of the NEDD8 conjugation system by a splicing variant, NUB1L. J Biol Chem. 2003;278:32905–32913.
- Su V, Lau AF. Ubiquitin-like and ubiquitin-associated domain proteins: significance in proteasomal degradation. Cell Mol Life Sci. 2009;66:2819–2833.
- Tanji K, Tanaka T, Mori F, et al. NUB1 suppresses the formation of Lewy body-like inclusions by proteasomal degradation of synphilin-1. Am J Pathol. 2006;169:553–565.
- Richet E, Pooler AM, Rodriguez T, et al. NUB1 modulation of GSK3beta reduces tau aggregation. Hum Mol Genet. 2012;21:5254–5267.
- Hosono T, Tanaka T, Tanji K, Nakatani T, Kamitani T. NUB1, an interferon-inducible protein, mediates anti-proliferative actions and apoptosis in renal cell carcinoma cells through cell-cycle regulation. Br J Cancer. 2010;102:873–882.
- Kaltenbach LS, Romero E, Becklin RR, et al. Huntingtin interacting proteins are genetic modifiers of neurodegeneration. PLoS Genet. 2007;3:e82.
- Kamitani T, Kito K, Fukuda-Kamitani T, Yeh ET. Targeting of NEDD8 and its conjugates for proteasomal degradation by NUB1. J Biol Chem. 2001;276:46655–46660.
- Tanaka T, Yeh ET, Kamitani T. NUB1-mediated targeting of the ubiquitin precursor UbC1 for its C-terminal hydrolysis. Eur J Biochem. 2004;271:972–982.
- Tanji K, Tanaka T, Kamitani T. Interaction of NUB1 with the proteasome subunit S5a. Biochem Biophys Res Commun. 2005;337:116–120.
- Tanaka T, Nakatani T, Kamitani T. Inhibition of NEDD8-conjugation pathway by novel molecules: potential approaches to anticancer therapy. Mol Oncol. 2012;6:267–275.
- Rabut G, Peter M. Function and regulation of protein neddylation. ‘Protein modifications: beyond the usual suspects’ review series. EMBO Rep. 2008;9:969–976.
- Hipp MS, Raasi S, Groettrup M, Schmidtke G. NEDD8 ultimate buster-1L interacts with the ubiquitin-like protein FAT10 and accelerates its degradation. J Biol Chem. 2004;279:16503–16510.
- Schmidtke G, Kalveram B, Weber E, et al. The UBA domains of NUB1L are required for binding but not for accelerated degradation of the ubiquitin-like modifier FAT10. J Biol Chem. 2006;281:20045–20054.
- Pan ZQ, Kentsis A, Dias DC, Yamoah K, Wu K. Nedd8 on cullin: building an expressway to protein destruction. Oncogene. 2004;23:1985–1997.
- Wimuttisuk W, Singer JD. The Cullin3 ubiquitin ligase functions as a Nedd8-bound heterodimer. Mol Biol Cell. 2007;18:899–909.
- Choo YY, Hagen T. Mechanism of cullin3 E3 ubiquitin ligase dimerization. PLoS One. 2012;7:e41350.
- Metzger T, Kleiss C, Sumara I. CUL3 and protein kinases: insights from PLK1/KLHL22 interaction. Cell Cycle. 2013;12:2291–2296.
- Tanji K, Mori F, Kito K, et al. Synphilin-1-binding protein NUB1 is colocalized with nonfibrillar, proteinase K-resistant α-synuclein in presynapses in Lewy body disease. J Neuropathol Exp Neurol. 2011;70:879–889.
- Chort A, Alves S, Marinello M, et al. Interferon β induces clearance of mutant ataxin 7 and improves locomotion in SCA7 knock-in mice. Brain. 2013;136:1732–1745.
- Comi G, Filippi M, Barkhof F, et al. Effect of early interferon treatment on conversion to definite multiple sclerosis: a randomised study. Lancet. 2001;357:1576–1582.
- Goëb J, Cailleau A, Lainé P, et al. Acute delirium, delusion, and depression during IFN-beta-1a therapy for multiple sclerosis: a case report. Clin Neuropharmacol. 2003;26:5–7.
- Kremenchutzky M, Morrow S, Rush C. The safety and efficacy of IFN-beta products for the treatment of multiple sclerosis. Expert Opin Drug Saf. 2007;6:279–288.
- Leuschen MP, Filipi M, Healey K. A randomized open label study of pain medications (naproxen, acetaminophen and ibuprofen) for controlling side effects during initiation of IFN beta-1a therapy and during its ongoing use for relapsing-remitting multiple sclerosis. Mult Scler. 2004;10:636–642.
- Boute N, Jockers R, Issad T. The use of resonance energy transfer in high-throughput screening: BRET versus FRET. Trends Pharmacol Sci. 2002;23:351–354.
- Cochran JN, Diggs PV, Nebane NM, et al. AlphaScreen HTS and live-cell bioluminescence resonance energy transfer (BRET) assays for identification of Tau-Fyn SH3 interaction inhibitors for Alzheimer disease. J Biomol Screen. 2014;19:1338–1349.
- Schwechheimer C, Deng XW. COP9 signalosome revisited: a novel mediator of protein degradation. Trends Cell Biol. 2001;11:420–426.
- Pintard L, Kurz T, Glaser S, Willis JH, Peter M, Bowerman B. Neddylation and deneddylation of CUL-3 is required to target MEI-1/Katanin for degradation at the meiosis-to-mitosis transition in C. elegans. Curr Biol. 2003;13:911–921.
- Wee S, Geyer RK, Toda T, Wolf DA. CSN facilitates Cullin-RING ubiquitin ligase function by counteracting autocatalytic adapter instability. Nat Cell Biol. 2005;7:387–391.
- Wu JT, Chan YR, Chien CT. Protection of cullin-RING E3 ligases by CSN-UBP12. Trends Cell Biol. 2006;16:362–369.
- Wu JT, Lin HC, Hu YC, Chien CT. Neddylation and deneddylation regulate Cul1 and Cul3 protein accumulation. Nat Cell Biol. 2005;7:1014–1020.
- Enchev RI, Scott DC, da Fonseca PC, et al. Structural basis for a reciprocal regulation between SCF and CSN. Cell Rep. 2012;2:616–627.
- Gan-Erdene T, Nagamalleswari K, Yin L, Wu K, Pan ZQ, Wilkinson KD. Identification and characterization of DEN1, a deneddylase of the ULP family. J Biol Chem. 2003;278:28892–28900.
- Gong L, Kamitani T, Millas S, Yeh ET. Identification of a novel isopeptidase with dual specificity for ubiquitin- and NEDD8-conjugated proteins. J Biol Chem. 2000;275:14212–14216.
- Hemelaar J, Borodovsky A, Kessler BM, et al. Specific and covalent targeting of conjugating and deconjugating enzymes of ubiquitin-like proteins. Mol Cell Biol. 2004;24:84–95.
- Wada H, Kito K, Caskey LS, Yeh ET, Kamitani T. Cleavage of the C-terminus of NEDD8 by UCH-L3. Biochem Biophys Res Commun. 1998;251:688–692.
- Mtango NR, Sutovsky M, Vandevoort CA, Latham KE, Sutovsky P. Essential role of ubiquitin C-terminal hydrolases UCHL1 and UCHL3 in mammalian oocyte maturation. J Cell Physiol. 2012;227:2022–2029.
- Kordasiewicz HB, Stanek LM, Wancewicz EV, et al. Sustained therapeutic reversal of Huntington’s disease by transient repression of huntingtin synthesis. Neuron. 2012;74:1031–1044.