SUMO-targeted ubiquitin ligases
| Autor: | Annie M. Sriramachandran, R. Jürgen Dohmen |
|---|---|
| Rok vydání: | 2014 |
| Předmět: |
DNA Repair
Ubiquitin-Protein Ligases Slx5 SUMO-1 Protein SUMO protein SUMO enzymes Saccharomyces cerevisiae Rnf4 Genomic Instability Ubiquitin Yeasts Schizosaccharomyces Animals Humans Molecular Biology biology Uls1 Sumoylation SIM Cell Biology Subcellular localization Arkadia Ubiquitin ligase Cell biology Proteasome Proteolysis biology.protein Posttranslational modification Slx8 Function (biology) DNA Damage |
| Zdroj: | Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 1843:75-85 |
| ISSN: | 0167-4889 |
| DOI: | 10.1016/j.bbamcr.2013.08.022 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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