Ubc9 fusion-directed SUMOylation identifies constitutive and inducible SUMOylation

Ubc9 fusion-directed SUMOylation identifies constitutive and inducible SUMOylation

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...

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Main Authors: Jakobs, Astrid, Himstedt, Fabian, Funk, Martin, Korn, Bernhard, Gaestel, Matthias, Niedenthal, Rainer
Format: Online
Language:English
Published: Oxford University Press 2007
Online Access:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2034454/
id pubmed-2034454
recordtype oai_dc
spelling pubmed-20344542007-10-24 Ubc9 fusion-directed SUMOylation identifies constitutive and inducible SUMOylation Jakobs, Astrid Himstedt, Fabian Funk, Martin Korn, Bernhard Gaestel, Matthias Niedenthal, Rainer Methods Online 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. Oxford University Press 2007-09 2007-08-20 /pmc/articles/PMC2034454/ /pubmed/17709345 http://dx.doi.org/10.1093/nar/gkm617 Text en © 2007 The Author(s) http://creativecommons.org/licenses/by-nc/2.0/uk/ 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.
repository_type Open Access Journal
institution_category Foreign Institution
institution US National Center for Biotechnology Information
building NCBI PubMed
collection Online Access
language English
format Online
author Jakobs, Astrid
Himstedt, Fabian
Funk, Martin
Korn, Bernhard
Gaestel, Matthias
Niedenthal, Rainer
spellingShingle Jakobs, Astrid
Himstedt, Fabian
Funk, Martin
Korn, Bernhard
Gaestel, Matthias
Niedenthal, Rainer
Ubc9 fusion-directed SUMOylation identifies constitutive and inducible SUMOylation
author_facet Jakobs, Astrid
Himstedt, Fabian
Funk, Martin
Korn, Bernhard
Gaestel, Matthias
Niedenthal, Rainer
author_sort Jakobs, Astrid
title Ubc9 fusion-directed SUMOylation identifies constitutive and inducible SUMOylation
title_short Ubc9 fusion-directed SUMOylation identifies constitutive and inducible SUMOylation
title_full Ubc9 fusion-directed SUMOylation identifies constitutive and inducible SUMOylation
title_fullStr Ubc9 fusion-directed SUMOylation identifies constitutive and inducible SUMOylation
title_full_unstemmed Ubc9 fusion-directed SUMOylation identifies constitutive and inducible SUMOylation
title_sort ubc9 fusion-directed sumoylation identifies constitutive and inducible sumoylation
description 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.
publisher Oxford University Press
publishDate 2007
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2034454/
_version_ 1611405299445399552

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