Proteasomes can degrade a significant proportion of cellular proteins independent of ubiquitination.

@article{Baugh2009ProteasomesCD,
  title={Proteasomes can degrade a significant proportion of cellular proteins independent of ubiquitination.},
  author={James M Baugh and Ekaterina G. Viktorova and Evgeny V. Pilipenko},
  journal={Journal of molecular biology},
  year={2009},
  volume={386 3},
  pages={814-27}
}
The critical role of the ubiquitin-26S proteasome system in regulation of protein homeostasis in eukaryotes is well established. In contrast, the impact of the ubiquitin-independent proteolytic activity of proteasomes is poorly understood. Through biochemical analysis of mammalian lysates, we find that the 20S proteasome, latent in peptide hydrolysis, specifically cleaves more than 20% of all cellular proteins. Thirty intrinsic proteasome substrates (IPSs) were identified and in vitro studies… CONTINUE READING

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Functions of the proteasome: from protein degradation and immune surveillance to cancer therapy

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