| Literature DB >> 24018209 |
Annie M Sriramachandran1, R Jürgen Dohmen.
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
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Year: 2013 PMID: 24018209 DOI: 10.1016/j.bbamcr.2013.08.022
Source DB: PubMed Journal: Biochim Biophys Acta ISSN: 0006-3002