A copy of this work was available on the public web and has been preserved in the Wayback Machine. The capture dates from 2019; you can also visit the original URL.
The file type is application/pdf
.
Huntingtin toxicity in yeast model depends on polyglutamine aggregation mediated by a prion-like protein Rnq1
2002
Journal of Cell Biology
he cause of Huntington's disease is expansion of polyglutamine (polyQ) domain in huntingtin, which makes this protein both neurotoxic and aggregation prone. Here we developed the first yeast model, which establishes a direct link between aggregation of expanded polyQ domain and its cytotoxicity. Our data indicated that deficiencies in molecular chaperones Sis1 and Hsp104 inhibited seeding of polyQ aggregates, whereas ssa1 , ssa2 , and ydj1-151 mutations inhibited expansion of aggregates. The
doi:10.1083/jcb.200112104
pmid:12058016
pmcid:PMC2174031
fatcat:fcxwz3nhgzhwlmr4uoofodq4xa