Mechanisms for regulating deubiquitinating enzymes

Protein Sci. 2014 Apr;23(4):344-53. doi: 10.1002/pro.2415. Epub 2014 Feb 12.

Abstract

Ubiquitination is a reversible post-translational modification that plays a dynamic role in regulating most eukaryotic processes. Deubiquitinating enzymes (DUBs), which hydrolyze the isopeptide or peptide linkages joining ubiquitin to substrate lysines or N-termini, therefore play a key role in ubiquitin signaling. Cells employ multiple mechanisms to regulate DUB activity and thus ensure the appropriate biological response. Recent structural studies have shed light on several different mechanisms by which DUB activity and specificity is regulated.

Keywords: DUB; UBL; deubiquitinating enzymes; ubiquitin.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Review

MeSH terms

  • Humans
  • Models, Molecular
  • Peptides / chemistry
  • Peptides / metabolism
  • Signal Transduction
  • Ubiquitin / chemistry
  • Ubiquitin / metabolism
  • Ubiquitin-Specific Proteases / chemistry
  • Ubiquitin-Specific Proteases / genetics
  • Ubiquitin-Specific Proteases / metabolism*
  • Ubiquitination

Substances

  • Peptides
  • Ubiquitin
  • Ubiquitin-Specific Proteases