Deubiquitinating enzymes as cellular regulators

J Biochem. 2003 Jul;134(1):9-18. doi: 10.1093/jb/mvg107.


Modification of proteins by the covalent attachment of ubiquitin is a key regulatory mechanism of many cellular processes including protein degradation by the 26S proteasome. Deubiquitination, reversal of this modification, must also regulate the fate and function of ubiquitin-conjugated proteins. Deubiquitinating enzymes catalyze the removal of ubiquitin from ubiquitin-conjugated substrate proteins as well as from its precursor proteins. Deubiquitinating enzymes occupy the largest family of enzymes in the ubiquitin system, implying their diverse function in regulation of the ubiquitin-mediated pathways. Here we explore the diversity of deubiquitinating enzymes and their emerging roles as cellular regulators.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Cysteine Endopeptidases / chemistry
  • Cysteine Endopeptidases / physiology*
  • Endopeptidases / chemistry
  • Endopeptidases / physiology*
  • Humans
  • Multienzyme Complexes / chemistry
  • Multienzyme Complexes / physiology*
  • Transcription, Genetic
  • Ubiquitin Thiolesterase / chemistry
  • Ubiquitin Thiolesterase / physiology*
  • Ubiquitins / metabolism*


  • Multienzyme Complexes
  • Ubiquitins
  • Endopeptidases
  • Ubiquitin Thiolesterase
  • Cysteine Endopeptidases
  • ubiquitin-Nalpha-protein hydrolase