Accumulation of mutant huntingtin fragments in aggresome-like inclusion bodies as a result of insufficient protein degradation.

@article{Waelter2001AccumulationOM,
  title={Accumulation of mutant huntingtin fragments in aggresome-like inclusion bodies as a result of insufficient protein degradation.},
  author={S. Waelter and A. Boeddrich and R. Lurz and E. Scherzinger and G. Lueder and H. Lehrach and E. Wanker},
  journal={Molecular biology of the cell},
  year={2001},
  volume={12 5},
  pages={
          1393-407
        }
}
The huntingtin exon 1 proteins with a polyglutamine repeat in the pathological range (51 or 83 glutamines), but not with a polyglutamine tract in the normal range (20 glutamines), form aggresome-like perinuclear inclusions in human 293 Tet-Off cells. [...] Key Result Inhibition of proteasome activity resulted in a twofold increase in the amount of ubiquitinated, SDS-resistant aggregates, indicating that inclusion bodies accumulate when the capacity of the ubiquitin-proteasome system to degrade aggregation-prone…Expand
Detection of ubiquitinated huntingtin species in intracellular aggregates
Heat shock protein 70 alters the endosome-lysosomal localization of huntingtin
Amyloid precursor protein accumulates in aggresomes in response to proteasome inhibitor
Leucine-Rich Repeat Kinase 2 Expression Leads to Aggresome Formation That Is Not Associated With &agr;-Synuclein Inclusions
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