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Gene Review

ATXN3  -  ataxin 3

Homo sapiens

Synonyms: AT3, ATX3, Ataxin-3, JOS, MJD, ...
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Disease relevance of ATXN3


Psychiatry related information on ATXN3


High impact information on ATXN3


Chemical compound and disease context of ATXN3


Biological context of ATXN3


Anatomical context of ATXN3

  • However, in 293 cells HHR23A is recruited to intranuclear inclusions formed by the mutant ataxin-3 through its interaction with ataxin-3 [18].
  • Upon immunocytochemical analysis we detected NI in all of the thalamic nuclei of all of our SCA3 patients [20].
  • This lack of correlation may suggest that ataxin-3 immunopositive NI are not immediately decisive for the fate of affected nerve cells but rather represent unspecific and pathognomonic morphological markers of SCA3 [20].
  • At the level of the spinal cord, synaptic loss in the dorsal nuclei of Clarke characterized FA and MJD/SCA-3 [4].
  • In SCA-3, abnormal ataxin-3 is aggregated in neuronal nuclei, and in SCA-6, a mutated alpha1A-calcium channel protein is the likely cause of abnormal calcium channel function in Purkinje cells and in the death of these neurons [3].

Associations of ATXN3 with chemical compounds


Physical interactions of ATXN3

  • These differences in NI formation reflect specific protein interactions normally undertaken by ataxin-3, as both normal and mutant full-length ataxin-3 co-immunoprecipitate with CBP and sediment on density gradients as macromolecular complexes [24].

Co-localisations of ATXN3

  • Cellular studies show that endogenous AT3 colocalizes with aggresomes and preaggresome particles of the misfolded cystic fibrosis transmembrane regulator (CFTR) mutant CFTRDeltaF508 and associates with histone deacetylase 6 and dynein, proteins required for aggresome formation and transport of misfolded protein [25].

Regulatory relationships of ATXN3

  • These data suggest that a normal function of AT3 is to regulate flow through the ERAD pathway by modulating VCP-dependent extraction of proteins from the ER [26].
  • A familial factor independent of CAG repeat length influences age at onset of Machado-Joseph disease [27].

Other interactions of ATXN3


Analytical, diagnostic and therapeutic context of ATXN3


  1. The prevalence and wide clinical spectrum of the spinocerebellar ataxia type 2 trinucleotide repeat in patients with autosomal dominant cerebellar ataxia. Geschwind, D.H., Perlman, S., Figueroa, C.P., Treiman, L.J., Pulst, S.M. Am. J. Hum. Genet. (1997) [Pubmed]
  2. Ubiquitin-mediated sequestration of normal cellular proteins into polyglutamine aggregates. Donaldson, K.M., Li, W., Ching, K.A., Batalov, S., Tsai, C.C., Joazeiro, C.A. Proc. Natl. Acad. Sci. U.S.A. (2003) [Pubmed]
  3. The hereditary ataxias. Koeppen, A.H. J. Neuropathol. Exp. Neurol. (1998) [Pubmed]
  4. Synapses in the hereditary ataxias. Koeppen, A.H., Dickson, A.C., Lamarche, J.B., Robitaille, Y. J. Neuropathol. Exp. Neurol. (1999) [Pubmed]
  5. Down-regulation of heat shock protein 27 in neuronal cells and non-neuronal cells expressing mutant ataxin-3. Wen, F.C., Li, Y.H., Tsai, H.F., Lin, C.H., Li, C., Liu, C.S., Lii, C.K., Nukina, N., Hsieh, M. FEBS Lett. (2003) [Pubmed]
  6. Pathology of CAG repeat diseases. Yamada, M., Tsuji, S., Takahashi, H. Neuropathology : official journal of the Japanese Society of Neuropathology. (2000) [Pubmed]
  7. Aggregate-prone proteins are cleared from the cytosol by autophagy: therapeutic implications. Williams, A., Jahreiss, L., Sarkar, S., Saiki, S., Menzies, F.M., Ravikumar, B., Rubinsztein, D.C. Curr. Top. Dev. Biol. (2006) [Pubmed]
  8. Expression of a poly-glutamine-ataxin-3 transgene in orexin neurons induces narcolepsy-cataplexy in the rat. Beuckmann, C.T., Sinton, C.M., Williams, S.C., Richardson, J.A., Hammer, R.E., Sakurai, T., Yanagisawa, M. J. Neurosci. (2004) [Pubmed]
  9. Sleep disturbance in spinocerebellar ataxias: is the SCA3 mutation a cause of restless legs syndrome? Schöls, L., Haan, J., Riess, O., Amoiridis, G., Przuntek, H. Neurology (1998) [Pubmed]
  10. Cognitive impairments in Machado-Joseph disease. Kawai, Y., Takeda, A., Abe, Y., Washimi, Y., Tanaka, F., Sobue, G. Arch. Neurol. (2004) [Pubmed]
  11. Expanded polyglutamine protein forms nuclear inclusions and causes neural degeneration in Drosophila. Warrick, J.M., Paulson, H.L., Gray-Board, G.L., Bui, Q.T., Fischbeck, K.H., Pittman, R.N., Bonini, N.M. Cell (1998) [Pubmed]
  12. Expanded polyglutamine in the Machado-Joseph disease protein induces cell death in vitro and in vivo. Ikeda, H., Yamaguchi, M., Sugai, S., Aze, Y., Narumiya, S., Kakizuka, A. Nat. Genet. (1996) [Pubmed]
  13. Deubiquitinating function of ataxin-3: insights from the solution structure of the Josephin domain. Mao, Y., Senic-Matuglia, F., Di Fiore, P.P., Polo, S., Hodsdon, M.E., De Camilli, P. Proc. Natl. Acad. Sci. U.S.A. (2005) [Pubmed]
  14. Extrapyramidal motor signs in degenerative ataxias. Schöls, L., Peters, S., Szymanski, S., Krüger, R., Lange, S., Hardt, C., Riess, O., Przuntek, H. Arch. Neurol. (2000) [Pubmed]
  15. Pharmacological treatments of cerebellar ataxia. Ogawa, M. Cerebellum (2004) [Pubmed]
  16. 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., Breuer, P. Hum. Mol. Genet. (2006) [Pubmed]
  17. Muscle cramp in Machado-Joseph disease: altered motor axonal excitability properties and mexiletine treatment. Kanai, K., Kuwabara, S., Arai, K., Sung, J.Y., Ogawara, K., Hattori, T. Brain (2003) [Pubmed]
  18. Ataxin-3, the MJD1 gene product, interacts with the two human homologs of yeast DNA repair protein RAD23, HHR23A and HHR23B. Wang, G., Sawai, N., Kotliarova, S., Kanazawa, I., Nukina, N. Hum. Mol. Genet. (2000) [Pubmed]
  19. An isoform of ataxin-3 accumulates in the nucleus of neuronal cells in affected brain regions of SCA3 patients. Schmidt, T., Landwehrmeyer, G.B., Schmitt, I., Trottier, Y., Auburger, G., Laccone, F., Klockgether, T., Völpel, M., Epplen, J.T., Schöls, L., Riess, O. Brain Pathol. (1998) [Pubmed]
  20. Spinocerebellar Ataxia Type 3 (SCA3): Thalamic Neurodegeneration Occurs Independently from Thalamic Ataxin-3 Immunopositive Neuronal Intranuclear Inclusions. Rüb, U., de Vos, R.A., Brunt, E.R., Sebestény, T., Schöls, L., Auburger, G., Bohl, J., Ghebremedhin, E., Gierga, K., Seidel, K., den Dunnen, W., Heinsen, H., Paulson, H., Deller, T. Brain Pathol. (2006) [Pubmed]
  21. Pathological consequences of VCP mutations on human striated muscle. Hübbers, C.U., Clemen, C.S., Kesper, K., Böddrich, A., Hofmann, A., Kämäräinen, O., Tolksdorf, K., Stumpf, M., Reichelt, J., Roth, U., Krause, S., Watts, G., Kimonis, V., Wattjes, M.P., Reimann, J., Thal, D.R., Biermann, K., Evert, B.O., Lochmüller, H., Wanker, E.E., Schoser, B.G., Noegel, A.A., Schröder, R. Brain (2007) [Pubmed]
  22. Cerebellar degeneration in hereditary dentatorubral-pallidoluysian atrophy and Machado-Joseph disease. Kumada, S., Hayashi, M., Mizuguchi, M., Nakano, I., Morimatsu, Y., Oda, M. Acta Neuropathol. (2000) [Pubmed]
  23. An arginine/lysine-rich motif is crucial for VCP/p97-mediated modulation of ataxin-3 fibrillogenesis. Boeddrich, A., Gaumer, S., Haacke, A., Tzvetkov, N., Albrecht, M., Evert, B.O., Müller, E.C., Lurz, R., Breuer, P., Schugardt, N., Plassmann, S., Xu, K., Warrick, J.M., Suopanki, J., Wüllner, U., Frank, R., Hartl, U.F., Bonini, N.M., Wanker, E.E. EMBO J. (2006) [Pubmed]
  24. The role of protein composition in specifying nuclear inclusion formation in polyglutamine disease. Chai, Y., Wu, L., Griffin, J.D., Paulson, H.L. J. Biol. Chem. (2001) [Pubmed]
  25. The polyglutamine neurodegenerative protein ataxin 3 regulates aggresome formation. Burnett, B.G., Pittman, R.N. Proc. Natl. Acad. Sci. U.S.A. (2005) [Pubmed]
  26. Ataxin-3 binds VCP/p97 and regulates retrotranslocation of ERAD substrates. Zhong, X., Pittman, R.N. Hum. Mol. Genet. (2006) [Pubmed]
  27. A familial factor independent of CAG repeat length influences age at onset of Machado-Joseph disease. DeStefano, A.L., Cupples, L.A., Maciel, P., Gaspar, C., Radvany, J., Dawson, D.M., Sudarsky, L., Corwin, L., Coutinho, P., MacLeod, P. Am. J. Hum. Genet. (1996) [Pubmed]
  28. Elucidation of ataxin-3 and ataxin-7 function by integrative bioinformatics. Scheel, H., Tomiuk, S., Hofmann, K. Hum. Mol. Genet. (2003) [Pubmed]
  29. A family with Machado-Joseph disease, previously diagnosed as dentatorubral-pallidoluysian atrophy. Sakai, T., Antoku, Y., Kawakami, H., Maruyama, H., Nakamura, S., Tanaka, K. Neurology (1996) [Pubmed]
  30. Frequency analysis of autosomal dominant spinocerebellar ataxias in mainland Chinese patients and clinical and molecular characterization of spinocerebellar ataxia type 6. Jiang, H., Tang, B.S., Xu, B., Zhao, G.H., Shen, L., Tang, J.G., Li, Q.H., Xia, K. Chin. Med. J. (2005) [Pubmed]
  31. Identification of five spinocerebellar ataxia type 2 pedigrees in patients with autosomal dominant cerebellar ataxia in Taiwan. Hsieh, M., Li, S.Y., Tsai, C.J., Chen, Y.Y., Liu, C.S., Chang, C.Y., Ro, L.S., Chen, D.F., Chen, S.S., Li, C. Acta neurologica Scandinavica. (1999) [Pubmed]
  32. The occurrence of dominant spinocerebellar ataxias among 251 Finnish ataxia patients and the role of predisposing large normal alleles in a genetically isolated population. Juvonen, V., Hietala, M., Kairisto, V., Savontaus, M.L. Acta neurologica Scandinavica. (2005) [Pubmed]
  33. Non-expanded polyglutamine proteins in intranuclear inclusions of hereditary ataxias--triple-labeling immunofluorescence study. Uchihara, T., Fujigasaki, H., Koyano, S., Nakamura, A., Yagishita, S., Iwabuchi, K. Acta Neuropathol. (2001) [Pubmed]
  34. Poly-ubiquitin binding by the polyglutamine disease protein ataxin-3 links its normal function to protein surveillance pathways. Chai, Y., Berke, S.S., Cohen, R.E., Paulson, H.L. J. Biol. Chem. (2004) [Pubmed]
  35. The natural history of degenerative ataxia: a retrospective study in 466 patients. Klockgether, T., Lüdtke, R., Kramer, B., Abele, M., Bürk, K., Schöls, L., Riess, O., Laccone, F., Boesch, S., Lopes-Cendes, I., Brice, A., Inzelberg, R., Zilber, N., Dichgans, J. Brain (1998) [Pubmed]
  36. Autosomal dominant cerebellar ataxia type I. Nerve conduction and evoked potential studies in families with SCA1, SCA2 and SCA3. Abele, M., Bürk, K., Andres, F., Topka, H., Laccone, F., Bösch, S., Brice, A., Cancel, G., Dichgans, J., Klockgether, T. Brain (1997) [Pubmed]
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