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Nucleic Acids Research Advance Access published online on August 20, 2007
Nucleic Acids Research, doi:10.1093/nar/gkm617
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© 2007 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

Methods Online

Ubc9 fusion-directed SUMOylation identifies constitutive and inducible SUMOylation

Astrid Jakobs1, Fabian Himstedt1, Martin Funk2, Bernhard Korn3, Matthias Gaestel1 and Rainer Niedenthal1,*

1Institut für Physiologische Chemie, Medizinische Hochschule Hannover, Carl-Neuberg Street, 1, 30625 Hannover, 2MediGene AG, Lochhamer Street, 11, 82152 Martinsried and 3Deutsches Krebsforschungszentrum, Genomics and Proteomics Core Facilities, Im Neuenheimer Feld 515, 69120 Heidelberg, Germany

*To whom correspondence should be addressed. Tel: +0511 532 2826; Fax: +0511 532 2827; Email: niedenthal.rainer{at}mh-hannover.de

Received May 30, 2007. Revised July 27, 2007. Accepted July 28, 2007.

Constitutive and induced protein SUMOylation is involved in the regulation of a variety of cellular processes, such as regulation of gene expression and protein transport, and proceeds mainly in the nucleus of the cell. So far, several hundred SUMOylation targets have been identified, but presumably they represent only a part of the total of proteins which are regulated by SUMOylation. Here, we used the Ubc9 fusion-dependent SUMOylation system (UFDS) to screen for constitutive and induced SUMOylation of 46 randomly chosen proteins with proven or potential nuclear localization. Fourteen new UFDS-substrate proteins were identified of which eight could be demonstrated to be SUMOylated in a UFDS-independent manner in vivo. Of these, three were constitutively SUMOylated (FOS, CRSP9 and CDC37) while the remaining five substrates (CSNK2B, TAF10, HSF2BP, PSMC3 and DRG1) showed a stimulation-dependent SUMOylation induced by the MAP3 kinase MEKK1. Hence, UFDS is appropriate for the identification and characterization of constitutive and, more importantly, induced protein SUMOylation in vivo.


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