To degrade or release: ubiquitin-chain remodeling

Trends Cell Biol. 2007 Sep;17(9):419-21. doi: 10.1016/j.tcb.2007.06.008. Epub 2007 Sep 27.

Abstract

The proteasome controls many cellular processes by degrading a large number of regulatory proteins. Most proteins are targeted to the proteasome through covalent tagging by a chain consisting of several copies of the small protein ubiquitin. Finley and coworkers have now discovered two proteins, Hul5 and Ubp6, which regulate degradation further, when bound to the proteasome. Hul5 promotes degradation by extending the number of ubiquitin moieties in the tag on substrates, whereas Ubp6 antagonizes degradation by trimming ubiquitin from the tag. The balance between these two opposing activities might control the substrate specificity of the proteasome and adjusting the balance would provide a new level of degradation control.

MeSH terms

  • Endopeptidases / metabolism
  • Models, Biological
  • Polyubiquitin / metabolism*
  • Proteasome Endopeptidase Complex / metabolism*
  • Saccharomyces cerevisiae Proteins / metabolism
  • Substrate Specificity
  • Ubiquitin-Protein Ligases / metabolism

Substances

  • Saccharomyces cerevisiae Proteins
  • Polyubiquitin
  • HUL5 protein, S cerevisiae
  • Ubiquitin-Protein Ligases
  • Endopeptidases
  • Proteasome Endopeptidase Complex
  • UBP6 protein, S cerevisiae