SUMO-targeted ubiquitin ligases

被引：200

作者：

Sriramachandran, Annie M. ^{[1
]}

Dohmen, R. Juergen ^{[1
]}

机构：

[1] Univ Cologne, Inst Genet, D-50674 Cologne, Germany

来源：

BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH | 2014年 / 1843卷 / 01期

关键词：

Rnf4; Arkadia; Uls1; Slx5; Slx8; SlM; RING FINGER PROTEIN; IN-VIVO IDENTIFICATION; DNA-DAMAGE; E3; LIGASE; HOMOLOGOUS RECOMBINATION; SACCHAROMYCES-CEREVISIAE; TRANSCRIPTIONAL ACTIVITY; SYNAPTONEMAL COMPLEX; MASS-SPECTROMETRY; INTERACTING MOTIF;

D O I：

10.1016/j.bbamcr.2013.08.022

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：75 / 85

页数：11

共 164 条

[1]

Abed M., 2011, FLY AUSTIN, V5

[2] Degringolade, a SUMO-targeted ubiquitin ligase, inhibits Hairy/Groucho-mediated repression [J].

Abed, Mona ;

Barry, Kevin C. ;

Kenyagin, Dorit ;

Koltun, Bella ;

Phippen, Taryn M. ;

Delrow, Jeffrey J. ;

Parkhurst, Susan M. ;

Orian, Amir .

EMBO JOURNAL, 2011, 30 (07) :1289-1301

[3] Small heat shock proteins target mutant cystic fibrosis transmembrane conductance regulator for degradation via a small ubiquitin-like modifier-dependent pathway [J].

Ahner, Annette ;

Gong, Xiaoyan ;

Schmidt, Bela Z. ;

Peters, Kathryn W. ;

Rabeh, Wael M. ;

Thibodeau, Patrick H. ;

Lukacs, Gergely L. ;

Frizzell, Raymond A. .

MOLECULAR BIOLOGY OF THE CELL, 2013, 24 (02) :74-84

[4] Yeast as a model system to study RecQ helicase function [J].

Ashton, Thomas M. ;

Hickson, Ian D. .

DNA REPAIR, 2010, 9 (03) :303-314

[5] The Drosophila STUbL protein Degringolade limits HES functions during embryogenesis [J].

Barry, Kevin C. ;

Abed, Mona ;

Kenyagin, Dorit ;

Werwie, Timothy R. ;

Boico, Olga ;

Orian, Amir ;

Parkhurst, Susan M. .

DEVELOPMENT, 2011, 138 (09) :1759-1769

[6] Role of Cdc48/p97 as a SUMO-targeted segregase curbing Rad51-Rad52 interaction [J].

Bergink, Steven ;

Ammon, Tim ;

Kern, Maximilian ;

Schermelleh, Lothar ;

Leonhardt, Heinrich ;

Jentsch, Stefan .

NATURE CELL BIOLOGY, 2013, 15 (05) :526-+

[7] Principles of ubiquitin and SUMO modifications in DNA repair [J].

Bergink, Steven ;

Jentsch, Stefan .

NATURE, 2009, 458 (7237) :461-467

[8] In Vivo Identification of Sumoylation Sites by a Signature Tag and Cysteine-targeted Affinity Purification [J].

Blomster, Henri A. ;

Imanishi, Susumu Y. ;

Siimes, Jenny ;

Kastu, Juha ;

Morrice, Nick A. ;

Eriksson, John E. ;

Sistonen, Lea .

JOURNAL OF BIOLOGICAL CHEMISTRY, 2010, 285 (25) :19324-19329

[9] Reciprocal activities between herpes simplex virus type 1 regulatory protein ICP0, a ubiquitin E3 ligase, and ubiquitin-specific protease USP7 [J].

Boutell, C ;

Canning, M ;

Orr, A ;

Everett, RD .

JOURNAL OF VIROLOGY, 2005, 79 (19) :12342-12354

[10] The herpes simplex virus type 1 (HSV-1) regulatory protein ICP0 interacts with and ubiquitinates p53 [J].

Boutell, C ;

Everett, RD .

JOURNAL OF BIOLOGICAL CHEMISTRY, 2003, 278 (38) :36596-36602

← 1 2 3 4 5 6 7 8 9 10 →