SUMO-targeted Ubiquitin Ligases

Biochim Biophys Acta. 2014 Jan;1843(1):75-85. doi: 10.1016/j.bbamcr.2013.08.022. Epub 2013 Sep 7.

Abstract

Covalent posttranslational modification with SUMO (small ubiquitin-related modifier) modulates functions of a wide range of proteins in eukaryotic cells. Sumoylation affects the activity, interaction properties, subcellular localization and the stability of its substrate proteins. The recent discovery of a novel class of ubiquitin ligases (E3), termed ULS (E3-S) or STUbL, that recognize sumoylated proteins, links SUMO modification to the ubiquitin/proteasome system. Here we review recent insights into the properties and function of these ligases and their roles in regulating sumoylated proteins. This article is part of a Special Issue entitled: Ubiquitin-Proteasome System. Guest Editors: Thomas Sommer and Dieter H. Wolf.

Keywords: Arkadia; Rnf4; SIM; Slx5; Slx8; Uls1.

Publication types

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

MeSH terms

  • Animals
  • DNA Damage / physiology
  • DNA Repair / physiology
  • Genomic Instability / physiology
  • Humans
  • Proteolysis
  • SUMO-1 Protein / metabolism*
  • Saccharomyces cerevisiae / enzymology
  • Schizosaccharomyces / enzymology
  • Sumoylation*
  • Ubiquitin-Protein Ligases / metabolism*
  • Yeasts / enzymology

Substances

  • SUMO-1 Protein
  • Ubiquitin-Protein Ligases