Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10802184 | Biochimica et Biophysica Acta (BBA) - Molecular Cell Research | 2014 | 11 Pages |
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.
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Authors
Annie M. Sriramachandran, R. Jürgen Dohmen,