Universität zu Köln

Sriramachandran, Annie M. and Dohmen, R. Juergen ORCID: 0000-0002-5756-6780 (2014). SUMO-targeted ubiquitin ligases. Biochim. Biophys. Acta-Mol. Cell Res., 1843 (1). S. 75 - 86. AMSTERDAM: ELSEVIER SCIENCE BV. ISSN 1879-2596

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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. (C) 2013 The Authors. Published by Elsevier B.V. All rights reserved.

Item Type:	Journal Article
Creators:	Creators Email ORCID ORCID Put Code Sriramachandran, Annie M. UNSPECIFIED UNSPECIFIED UNSPECIFIED Dohmen, R. Juergen UNSPECIFIED orcid.org/0000-0002-5756-6780 UNSPECIFIED
URN:	urn:nbn:de:hbz:38-450999
DOI:	10.1016/j.bbamcr.2013.08.022
Journal or Publication Title:	Biochim. Biophys. Acta-Mol. Cell Res.
Volume:	1843
Number:	1
Page Range:	S. 75 - 86
Date:	2014
Publisher:	ELSEVIER SCIENCE BV
Place of Publication:	AMSTERDAM
ISSN:	1879-2596
Language:	English
Faculty:	Faculty of Mathematics and Natural Sciences
Divisions:	Faculty of Mathematics and Natural Sciences > Department of Biology > Institute for Genetics
Subjects:	no entry
Uncontrolled Keywords:	Keywords Language RING FINGER PROTEIN; IN-VIVO IDENTIFICATION; DNA-DAMAGE; E3 LIGASE; HOMOLOGOUS RECOMBINATION; SACCHAROMYCES-CEREVISIAE; TRANSCRIPTIONAL ACTIVITY; SYNAPTONEMAL COMPLEX; MASS-SPECTROMETRY; INTERACTING MOTIF Multiple languages Biochemistry & Molecular Biology; Cell Biology Multiple languages
Refereed:	Yes
URI:	http://kups.ub.uni-koeln.de/id/eprint/45099