The E3 ubiquitin ligase UBE3C enhances proteasome processivity by ubiquitinating partially proteolyzed substrates.

@article{Chu2013TheEU,
  title={The E3 ubiquitin ligase UBE3C enhances proteasome processivity by ubiquitinating partially proteolyzed substrates.},
  author={Bernard W Chu and Kyle M. Kovary and Johan Guillaume and Ling-chun Chen and Mary N Teruel and Thomas J. Wandless},
  journal={The Journal of biological chemistry},
  year={2013},
  volume={288 48},
  pages={34575-87}
}
To maintain protein homeostasis, cells must balance protein synthesis with protein degradation. Accumulation of misfolded or partially degraded proteins can lead to the formation of pathological protein aggregates. Here we report the use of destabilizing domains, proteins whose folding state can be reversibly tuned using a high affinity ligand, as model substrates to interrogate cellular protein quality control mechanisms in mammalian cells using a forward genetic screen. Upon knockdown of… CONTINUE READING