Impairment of the ubiquitin-proteasome system by protein aggregation.

@article{Bence2001ImpairmentOT,
  title={Impairment of the ubiquitin-proteasome system by protein aggregation.},
  author={Neil F Bence and Radhika Sampat and Ron R. Kopito},
  journal={Science},
  year={2001},
  volume={292 5521},
  pages={1552-5}
}
Intracellular deposition of aggregated and ubiquitylated proteins is a prominent cytopathological feature of most neurodegenerative disorders. Whether protein aggregates themselves are pathogenic or are the consequence of an underlying molecular lesion is unclear. Here, we report that protein aggregation directly impaired the function of the ubiquitin-proteasome system. Transient expression of two unrelated aggregation-prone proteins, a huntingtin fragment containing a pathogenic polyglutamine… CONTINUE READING
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