Function and regulation of SUMO proteases

Nat Rev Mol Cell Biol. 2012 Dec;13(12):755-66. doi: 10.1038/nrm3478.

Abstract

Covalent attachment of small ubiquitin-like modifier (SUMO) to proteins is highly dynamic, and both SUMO-protein conjugation and cleavage can be regulated. Protein desumoylation is carried out by SUMO proteases, which control cellular mechanisms ranging from transcription and cell division to ribosome biogenesis. Recent advances include the discovery of two novel classes of SUMO proteases, insights regarding SUMO protease specificity, and revelations of previously unappreciated SUMO protease functions in several key cellular pathways. These developments, together with new connections between SUMO proteases and the recently discovered SUMO-targeted ubiquitin ligases (STUbLs), make this an exciting period to study these enzymes.

Publication types

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

MeSH terms

  • Animals
  • Endopeptidases / genetics
  • Endopeptidases / metabolism*
  • Gene Expression Regulation / physiology
  • Humans
  • Mice
  • Saccharomyces cerevisiae Proteins / metabolism
  • Signal Transduction / genetics
  • Signal Transduction / physiology
  • Small Ubiquitin-Related Modifier Proteins / genetics
  • Small Ubiquitin-Related Modifier Proteins / metabolism*
  • Ubiquitin-Protein Ligases / metabolism*

Substances

  • Saccharomyces cerevisiae Proteins
  • Small Ubiquitin-Related Modifier Proteins
  • Ubiquitin-Protein Ligases
  • Endopeptidases