title: SUMO-targeted ubiquitin ligases.
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.
authors.affiliation: University of Cologne, Institute for Genetics, Zülpicher Straße 47a, D-50674 Cologne, Germany.
authors.forename: Annie M
authors.initials: AM
authors.lastname: Sriramachandran
authors.forename: R Jürgen
authors.initials: RJ
authors.lastname: Dohmen
mesh_terms: D000818:Animals; D004249:DNA Damage / Q000502:physiology; D004260:DNA Repair / Q000502:physiology; D042822:Genomic Instability / Q000502:physiology; D006801:Humans; D059748:Proteolysis; D025842:SUMO-1 Protein / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000201:enzymology; D012568:Schizosaccharomyces / Q000201:enzymology; D058207:Sumoylation; D044767:Ubiquitin-Protein Ligases / Q000378:metabolism*; D015003:Yeasts / Q000201:enzymology
chemical_list: D025842:SUMO-1 Protein; D044767:Ubiquitin-Protein Ligases
keywords: Arkadia; Rnf4; SIM; Slx5; Slx8; Uls1