The deubiquitinase ataxin-3 requires Rad23 and DnaJ-1 for its neuroprotective role in Drosophila melanogaster
Neurobiology of Disease, ISSN: 0969-9961, Vol: 82, Page: 12-21
2015
- 44Citations
- 43Captures
- 1Mentions
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- Citations44
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- Readers43
- 43
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The deubiquitinase ataxin-3 requires Rad23 and DnaJ-1 for its neuroprotective role in Drosophila melanogaster.
Authors: Wei-Ling Tsou, Michelle Ouyang, Ryan R Hosking, Joanna R Sutton, Jessica R Blount, Aaron A Burr, Sokol V Todi PMID: 26007638 DOI: 10.1016/j.nbd.2015.05.010 Publication
Article Description
Ataxin-3 is a deubiquitinase and polyglutamine (polyQ) disease protein with a protective role in Drosophila melanogaster models of neurodegeneration. In the fruit fly, wild-type ataxin-3 suppresses toxicity from several polyQ disease proteins, including a pathogenic version of itself that causes spinocerebellar ataxia type 3 and pathogenic huntingtin, which causes Huntington's disease. The molecular partners of ataxin-3 in this protective function are unclear. Here, we report that ataxin-3 requires its direct interaction with the ubiquitin-binding and proteasome-associated protein, Rad23 (known as hHR23A/B in mammals) in order to suppress toxicity from polyQ species in Drosophila. According to additional studies, ataxin-3 does not rely on autophagy or the proteasome to suppress polyQ-dependent toxicity in fly eyes. Instead this deubiquitinase, through its interaction with Rad23, leads to increased protein levels of the co-chaperone DnaJ-1 and depends on it to protect against degeneration. Through DnaJ-1, our data connect ataxin-3 and Rad23 to protective processes involved with protein folding rather than increased turnover of toxic polyQ species.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S0969996115001746; http://dx.doi.org/10.1016/j.nbd.2015.05.010; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=84930959583&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/26007638; https://linkinghub.elsevier.com/retrieve/pii/S0969996115001746; https://dx.doi.org/10.1016/j.nbd.2015.05.010
Elsevier BV
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