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• W2016332933 abstract "The causes of amyotrophic lateral sclerosis (ALS), a devastating human neurodegenerative disease, are poorly understood, although the protein TDP-43 has been suggested to have a critical role in disease pathogenesis. Here we show that ataxin 2 (ATXN2), a polyglutamine (polyQ) protein mutated in spinocerebellar ataxia type 2, is a potent modifier of TDP-43 toxicity in animal and cellular models. ATXN2 and TDP-43 associate in a complex that depends on RNA. In spinal cord neurons of ALS patients, ATXN2 is abnormally localized; likewise, TDP-43 shows mislocalization in spinocerebellar ataxia type 2. To assess the involvement of ATXN2 in ALS, we analysed the length of the polyQ repeat in the ATXN2 gene in 915 ALS patients. We found that intermediate-length polyQ expansions (27-33 glutamines) in ATXN2 were significantly associated with ALS. These data establish ATXN2 as a relatively common ALS susceptibility gene. Furthermore, these findings indicate that the TDP-43-ATXN2 interaction may be a promising target for therapeutic intervention in ALS and other TDP-43 proteinopathies." @default.
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• W2016332933 date "2010-08-01" @default.
• W2016332933 modified "2023-10-17" @default.
• W2016332933 title "Ataxin-2 intermediate-length polyglutamine expansions are associated with increased risk for ALS" @default.
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• W2016332933 doi "https://doi.org/10.1038/nature09320" @default.
• W2016332933 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2965417" @default.
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