Protein quality control: U-box-containing E3 ubiquitin ligases join the fold.

@article{Cyr2002ProteinQC,
  title={Protein quality control: U-box-containing E3 ubiquitin ligases join the fold.},
  author={Douglas M. Cyr and J{\"o}rg H{\"o}hfeld and C. G. Patterson},
  journal={Trends in biochemical sciences},
  year={2002},
  volume={27 7},
  pages={368-75}
}
Molecular chaperones act with folding co-chaperones to suppress protein aggregation and refold stress damaged proteins. However, it is not clear how slowly folding or misfolded polypeptides are targeted for proteasomal degradation. Generally, selection of proteins for degradation is mediated by E3 ubiquitin ligases of the mechanistically distinct HECT and RING domain sub-types. Recent studies suggest that the U-box protein family represents a third class of E3 enzymes. CHIP, a U-box-containing… CONTINUE READING