Work

SUMO-targeted ubiquitin ligases

Year: 2013

Type: article

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.

Source: Biochimica et Biophysica Acta (BBA) - Molecular Cell Research

DOI: 10.1016/j.bbamcr.2013.08.022

Authors: Annie M. Sriramachandran, R. Jürgen Dohmen

Institution: University of Cologne

Language: English

Topic: Ubiquitin and proteasome pathways

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: hybrid

Estimated APC paid: $3,930

Funder: Deutsche Forschungsgemeinschaft