G. Cancel, C. Duyckaerts, M. Holmberg, C. Zander, G. Yvert et al., Distribution of ataxin-7 in normal human brain and retina, Brain, vol.123, issue.12, pp.2519-2549, 2000.
DOI : 10.1093/brain/123.12.2519

A. Michalik and C. Van-broeckhoven, Pathogenesis of polyglutamine disorders: aggregation revisited. Human molecular genetics, 2003.

J. Gatchel and H. Zoghbi, Diseases of Unstable Repeat Expansion: Mechanisms and Common Principles, Nature Reviews Genetics, vol.101, issue.10, pp.743-55, 1038.
DOI : 10.1038/nrg1691

H. Orr and H. Zoghbi, Trinucleotide Repeat Disorders, Annual Review of Neuroscience, vol.30, issue.1, pp.575-621, 2007.
DOI : 10.1146/annurev.neuro.29.051605.113042

V. Weake, J. Dyer, C. Seidel, A. Box, S. Swanson et al., Post-transcription initiation function of the ubiquitous SAGA complex in tissue-specific gene activation, Genes & Development, vol.25, issue.14, pp.1499-509, 2011.
DOI : 10.1101/gad.2046211

J. Bonnet, C. Wang, T. Baptista, S. Vincent, W. Hsiao et al., The SAGA coactivator complex acts on the whole transcribed genome and is required for RNA polymerase II transcription, Genes & Development, vol.28, issue.18, pp.1999-2012, 2014.
DOI : 10.1101/gad.250225.114

J. Young, L. Gouw, S. Propp, B. Sopher, J. Taylor et al., Proteolytic Cleavage of Ataxin-7 by Caspase-7 Modulates Cellular Toxicity and Transcriptional Dysregulation, Journal of Biological Chemistry, vol.282, issue.41, pp.30150-60, 2007.
DOI : 10.1074/jbc.M705265200

G. Garden, R. Libby, Y. Fu, Y. Kinoshita, J. Huang et al., Polyglutamine-expanded ataxin-7 promotes non-cell-autonomous Purkinje cell degeneration and displays proteolytic cleavage in ataxic transgenic mice, J neurosci : off j Soc Neurosci, vol.22, issue.12, pp.4897-905, 2002.

S. Mookerjee, T. Papanikolaou, S. Guyenet, V. Sampath, A. Lin et al., Posttranslational Modification of Ataxin-7 at Lysine 257 Prevents Autophagy-Mediated Turnover of an N-Terminal Caspase-7 Cleavage Fragment, Journal of Neuroscience, vol.29, issue.48, pp.15134-15178, 2009.
DOI : 10.1523/JNEUROSCI.4720-09.2009

A. Janer, A. Werner, J. Takahashi-fujigasaki, A. Daret, H. Fujigasaki et al., SUMOylation attenuates the aggregation propensity and cellular toxicity of the polyglutamine expanded ataxin-7, Human Molecular Genetics, vol.19, issue.1, pp.181-95, 2010.
DOI : 10.1093/hmg/ddp478

C. Zander, J. Takahashi, E. Hachimi, K. Fujigasaki, H. Albanese et al., Similarities between spinocerebellar ataxia type 7 (SCA7) cell models and human brain: proteins recruited in inclusions and activation of caspase-3, Human Molecular Genetics, vol.10, issue.22, pp.2569-79, 2001.
DOI : 10.1093/hmg/10.22.2569

A. Mykowska, K. Sobczak, M. Wojciechowska, P. Kozlowski, and W. Krzyzosiak, CAG repeats mimic CUG repeats in the misregulation of alternative splicing, Nucleic Acids Research, vol.39, issue.20, pp.8938-51, 2011.
DOI : 10.1093/nar/gkr608

R. Nalavade, N. Griesche, D. Ryan, S. Hildebrand, and S. Krauss, Mechanisms of RNA-induced toxicity in CAG repeat disorders, Cell Death and Disease, vol.23, issue.8, 2013.
DOI : 10.1038/mt.2009.17

L. Spada, A. Fu, Y. Sopher, B. Libby, R. Wang et al., Polyglutamine-Expanded Ataxin-7 Antagonizes CRX Function and Induces Cone-Rod Dystrophy in a Mouse Model of SCA7, Neuron, vol.31, issue.6, pp.913-940, 2001.
DOI : 10.1016/S0896-6273(01)00422-6

S. Yoo, M. Pennesi, E. Weeber, B. Xu, R. Atkinson et al., SCA7 Knockin Mice Model Human SCA7 and Reveal Gradual Accumulation of Mutant Ataxin-7 in Neurons and Abnormalities in Short-Term Plasticity, Neuron, vol.37, issue.3, pp.383-401, 2003.
DOI : 10.1016/S0896-6273(02)01190-X

Y. Chen, J. Gatchel, R. Lewis, C. Mao, P. Grant et al., Gcn5 loss-of-function accelerates cerebellar and retinal degeneration in a SCA7 mouse model, Human Molecular Genetics, vol.21, issue.2, pp.394-405, 2012.
DOI : 10.1093/hmg/ddr474

L. De-almeida, C. Ross, D. Zala, P. Aebischer, and N. Deglon, Lentiviral-mediated delivery of mutant huntingtin in the striatum of rats induces a selective neuropathology modulated by polyglutamine repeat size, huntingtin expression levels, and protein length, J neurosci : off j Soc Neurosci, vol.22, issue.9, pp.3473-83, 2002.

S. Alves, E. Regulier, I. Nascimento-ferreira, R. Hassig, N. Dufour et al., Striatal and nigral pathology in a lentiviral rat model of Machado-Joseph disease, Human Molecular Genetics, vol.17, issue.14, pp.2071-83, 2008.
DOI : 10.1093/hmg/ddn106

C. Vance, B. Rogelj, T. Hortobagyi, D. Vos, K. Nishimura et al., Mutations in FUS, an RNA Processing Protein, Cause Familial Amyotrophic Lateral Sclerosis Type 6, Science, vol.323, issue.5918, pp.1208-1219, 2009.
DOI : 10.1126/science.1165942

J. Woulfe, D. Gray, and I. Mackenzie, FUS-Immunoreactive Intranuclear Inclusions in Neurodegenerative Disease, Brain Pathology, vol.33, issue.3, pp.589-97, 2010.
DOI : 10.1111/j.1750-3639.2009.00337.x

H. Doi, K. Okamura, P. Bauer, Y. Furukawa, H. Shimizu et al., RNA-binding Protein TLS Is a Major Nuclear Aggregate-interacting Protein in Huntingtin Exon 1 with Expanded Polyglutamine-expressing Cells, Journal of Biological Chemistry, vol.283, issue.10, pp.6489-500, 2008.
DOI : 10.1074/jbc.M705306200

M. Hasegawa, T. Arai, T. Nonaka, F. Kametani, M. Yoshida et al., Phosphorylated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis, Annals of Neurology, vol.127, issue.1, pp.60-70, 2008.
DOI : 10.1002/ana.21425

R. Fuentealba, M. Udan, S. Bell, I. Wegorzewska, J. Shao et al., Interaction with Polyglutamine Aggregates Reveals a Q/N-rich Domain in TDP-43, Journal of Biological Chemistry, vol.285, issue.34, pp.26304-26318, 2010.
DOI : 10.1074/jbc.M110.125039

M. Fardaei, M. Rogers, H. Thorpe, K. Larkin, M. Hamshere et al., Three proteins, MBNL, MBLL and MBXL, co-localize in vivo with nuclear foci of expanded-repeat transcripts in DM1 and DM2 cells, Human Molecular Genetics, vol.11, issue.7, pp.805-819, 2002.
DOI : 10.1093/hmg/11.7.805

A. Mankodi, C. Urbinati, Q. Yuan, R. Moxley, V. Sansone et al., Muscleblind localizes to nuclear foci of aberrant RNA in myotonic dystrophy types 1 and 2, Human Molecular Genetics, vol.10, issue.19, pp.2165-70, 2001.
DOI : 10.1093/hmg/10.19.2165

J. Miller, C. Urbinati, P. Teng-umnuay, M. Stenberg, B. Byrne et al., Recruitment of human muscleblind proteins to (CUG)n expansions associated with myotonic dystrophy, The EMBO Journal, vol.19, issue.17, pp.4439-4487, 2000.
DOI : 10.1093/emboj/19.17.4439

A. Chort, S. Alves, M. Marinello, B. Dufresnois, J. Dornbierer et al., Interferon beta induces clearance of mutant ataxin 7 and improves locomotion in SCA7 knock-in mice, Brain, vol.136, issue.6, pp.1732-1777, 2013.
DOI : 10.1093/brain/awt061

U. Rub, L. Schols, H. Paulson, G. Auburger, P. Kermer et al., Clinical features, neurogenetics and neuropathology of the polyglutamine spinocerebellar ataxias type 1, 2, 3, 6 and 7, Progress in Neurobiology, vol.104, pp.38-66, 2013.
DOI : 10.1016/j.pneurobio.2013.01.001

S. Alves, F. Cormier-dequaire, M. Marinello, T. Marais, M. Muriel et al., The autophagy/lysosome pathway is impaired in SCA7 patients and SCA7 knock-in mice, Acta Neuropathologica, vol.453, issue.Pt 12, pp.705-727, 2014.
DOI : 10.1007/s00401-014-1289-8

R. Kanadia, J. Shin, Y. Yuan, S. Beattie, T. Wheeler et al., Reversal of RNA missplicing and myotonia after muscleblind overexpression in a mouse poly(CUG) model for myotonic dystrophy, Proceedings of the National Academy of Sciences, vol.103, issue.31, pp.11748-53, 2006.
DOI : 10.1073/pnas.0604970103

L. Bianco, C. Ridet, J. Schneider, B. Deglon, N. Aebischer et al., ??-Synucleinopathy and selective dopaminergic neuron loss in a rat lentiviral-based model of Parkinson's disease, Proceedings of the National Academy of Sciences, vol.99, issue.16, pp.10813-10821, 2002.
DOI : 10.1073/pnas.152339799

E. Lauwers, Z. Debyser, J. Van-dorpe, D. Strooper, B. Nuttin et al., Neuropathology and Neurodegeneration in Rodent Brain Induced by Lentiviral Vectormediated Overexpression of ??-Synuclein, Brain Pathology, vol.15, issue.3, pp.364-72, 2003.
DOI : 10.1111/j.1750-3639.2003.tb00035.x

D. Kirik, L. Annett, C. Burger, N. Muzyczka, R. Mandel et al., Nigrostriatal ??-synucleinopathy induced by viral vector-mediated overexpression of human ??-synuclein: A new primate model of Parkinson's disease, Proceedings of the National Academy of Sciences, vol.100, issue.5, pp.2884-2893, 2003.
DOI : 10.1073/pnas.0536383100

G. Yvert, K. Lindenberg, D. Devys, D. Helmlinger, G. Landwehrmeyer et al., SCA7 mouse models show selective stabilization of mutant ataxin-7 and similar cellular responses in different neuronal cell types, Human Molecular Genetics, vol.10, issue.16, pp.1679-92, 2001.
DOI : 10.1093/hmg/10.16.1679

D. Merry, Y. Kobayashi, C. Bailey, A. Taye, and K. Fischbeck, Cleavage, aggregation and toxicity of the expanded androgen receptor in spinal and bulbar muscular atrophy, Human Molecular Genetics, vol.7, issue.4, pp.693-701, 1998.
DOI : 10.1093/hmg/7.4.693

L. Ellerby, A. Hackam, S. Propp, H. Ellerby, S. Rabizadeh et al., Kennedy's Disease, Journal of Neurochemistry, vol.15, issue.1, pp.185-95, 1999.
DOI : 10.1046/j.1471-4159.1999.0720185.x

C. Ross, Intranuclear Neuronal Inclusions: A Common Pathogenic Mechanism for Glutamine-Repeat Neurodegenerative Diseases?, Neuron, vol.19, issue.6, pp.1147-50, 1997.
DOI : 10.1016/S0896-6273(00)80405-5

C. Wellington, L. Ellerby, C. Gutekunst, D. Rogers, S. Warby et al., Caspase cleavage of mutant huntingtin precedes neurodegeneration in Huntington's disease, J neurosci : off j Soc Neurosci, vol.22, issue.18, pp.7862-72, 2002.

I. Klement, P. Skinner, M. Kaytor, H. Yi, S. Hersch et al., Ataxin-1 Nuclear Localization and Aggregation, Cell, vol.95, issue.1, pp.41-53, 1998.
DOI : 10.1016/S0092-8674(00)81781-X

U. Bichelmeier, T. Schmidt, J. Hubener, J. Boy, L. Ruttiger et al., Nuclear Localization of Ataxin-3 Is Required for the Manifestation of Symptoms in SCA3: In Vivo Evidence, Journal of Neuroscience, vol.27, issue.28, pp.7418-7446, 2007.
DOI : 10.1523/JNEUROSCI.4540-06.2007

M. Ito, Historical Review of the Significance of the Cerebellum and the Role of Purkinje Cells in Motor Learning, Annals of the New York Academy of Sciences, vol.80, issue.1 THE CEREBELLU, pp.273-88, 2002.
DOI : 10.1046/j.1460-9568.2002.02094.x

J. Sarna and R. Hawkes, Patterned Purkinje cell death in the cerebellum, Progress in Neurobiology, vol.70, issue.6, pp.473-507, 2003.
DOI : 10.1016/S0301-0082(03)00114-X

J. Barski, J. Hartmann, C. Rose, F. Hoebeek, K. Morl et al., Calbindin in cerebellar Purkinje cells is a critical determinant of the precision of motor coordination, J neurosci : off j Soc Neurosci, vol.23, issue.8, pp.3469-77, 2003.

J. Takahashi, H. Fujigasaki, C. Zander, E. Hachimi, K. Stevanin et al., Two populations of neuronal intranuclear inclusions in SCA7 differ in size and promyelocytic leukaemia protein content, Brain, vol.125, issue.7, pp.1534-1577, 2002.
DOI : 10.1093/brain/awf154

M. De-mezer, M. Wojciechowska, M. Napierala, K. Sobczak, and W. Krzyzosiak, Mutant CAG repeats of Huntingtin transcript fold into hairpins, form nuclear foci and are targets for RNA interference, Nucleic Acids Research, vol.39, issue.9, pp.3852-63, 2011.
DOI : 10.1093/nar/gkq1323

C. Reina, X. Zhong, and R. Pittman, Proteotoxic stress increases nuclear localization of ataxin-3. Human molecular genetics, pp.235-284, 2010.

H. Tsuiji, Y. Iguchi, A. Furuya, A. Kataoka, H. Hatsuta et al., Spliceosome integrity is defective in the motor neuron diseases ALS and SMA, EMBO Molecular Medicine, vol.133, issue.2, pp.221-255, 2013.
DOI : 10.1002/emmm.201202303

A. Blokhuis, E. Groen, M. Koppers, L. Van-den-berg, and R. Pasterkamp, Protein aggregation in amyotrophic lateral sclerosis, Acta Neuropathologica, vol.110, issue.Pt 15, pp.777-94, 2013.
DOI : 10.1007/s00401-013-1125-6

H. Doi, S. Koyano, Y. Suzuki, N. Nukina, and Y. Kuroiwa, The RNA-binding protein FUS/TLS is a common aggregate-interacting protein in polyglutamine diseases, Neuroscience Research, vol.66, issue.1, 2010.
DOI : 10.1016/j.neures.2009.10.004

T. Van-langenhove, J. Van-der-zee, K. Sleegers, S. Engelborghs, R. Vandenberghe et al., Genetic contribution of FUS to frontotemporal lobar degeneration, Neurology, vol.74, issue.5, pp.366-71, 2010.
DOI : 10.1212/WNL.0b013e3181ccc732

G. Klapstein, R. Fisher, H. Zanjani, C. Cepeda, E. Jokel et al., Electrophysiological and morphological changes in striatal spiny neurons in R6/2 Huntington's disease transgenic mice, J Neurophysiol, vol.86, issue.6, pp.2667-77, 2001.

R. Fujii, S. Okabe, T. Urushido, K. Inoue, A. Yoshimura et al., The RNA Binding Protein TLS Is Translocated to Dendritic Spines by mGluR5 Activation and Regulates Spine Morphology, Current Biology, vol.15, issue.6, pp.587-93, 2005.
DOI : 10.1016/j.cub.2005.01.058

F. Mori, Y. Toyoshima, K. Tanji, A. Kakita, H. Takahashi et al., FUS co-localizes with polyglutamine, but not with TDP-43 in neuronal intranuclear inclusions in spinocerebellar ataxia type 2, Neuropathol Appl Neurobiol

C. Schwab, T. Arai, M. Hasegawa, S. Yu, and P. Mcgeer, Colocalization of Transactivation-Responsive DNA-Binding Protein 43 and Huntingtin in Inclusions of Huntington Disease, Journal of Neuropathology & Experimental Neurology, vol.67, issue.12, pp.1159-65, 2008.
DOI : 10.1097/NEN.0b013e31818e8951

C. Tan, M. Yamada, Y. Toyoshima, A. Yokoseki, Y. Miki et al., Selective occurrence of TDP-43-immunoreactive inclusions in the lower motor neurons in Machado???Joseph disease, Acta Neuropathologica, vol.63, issue.4, pp.553-60, 2009.
DOI : 10.1007/s00401-009-0552-x

A. Clippinger, D. 'alton, S. Lin, W. Gendron, T. Howard et al., Robust cytoplasmic accumulation of phosphorylated TDP-43 in transgenic models of tauopathy, Acta Neuropathologica, vol.27, issue.39, pp.39-50, 2013.
DOI : 10.1007/s00401-013-1123-8

Y. Inukai, T. Nonaka, T. Arai, M. Yoshida, Y. Hashizume et al., Abnormal phosphorylation of Ser409/410 of TDP-43 in FTLD-U and ALS, FEBS Letters, vol.283, issue.19, pp.2899-904, 2008.
DOI : 10.1016/j.febslet.2008.07.027

M. Neumann, L. Kwong, E. Lee, E. Kremmer, A. Flatley et al., Phosphorylation of S409/410 of TDP-43 is a consistent feature in all sporadic and familial forms of TDP-43 proteinopathies, Acta Neuropathologica, vol.63, issue.2, pp.137-186, 2009.
DOI : 10.1007/s00401-008-0477-9

N. Liachko, P. Mcmillan, C. Guthrie, T. Bird, J. Leverenz et al., CDC7 inhibition blocks pathological TDP-43 phosphorylation and neurodegeneration, Annals of Neurology, vol.74, issue.1
DOI : 10.1002/ana.23870

Y. Nishimoto, D. Ito, T. Yagi, Y. Nihei, Y. Tsunoda et al., Characterization of Alternative Isoforms and Inclusion Body of the TAR DNA-binding Protein-43, Journal of Biological Chemistry, vol.285, issue.1, p.43
DOI : 10.1074/jbc.M109.022012

Y. Kino, C. Washizu, M. Kurosawa, Y. Oma, N. Hattori et al., Nuclear localization of MBNL1: splicing-mediated autoregulation and repression of