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      Regulation of transcription factors by sumoylation

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          ABSTRACT

          Transcription factors (TFs) are among the most frequently detected targets of sumoylation, and effects of the modification have been studied for about 200 individual TFs to date. TF sumoylation is most often associated with reduced target gene expression, which can be mediated by enhanced interactions with corepressors or by interference with protein modifications that promote transcription. However, recent studies show that sumoylation also regulates gene expression by controlling the levels of TFs that are associated with chromatin. SUMO can mediate this by modulating TF DNA-binding activity, promoting clearance of TFs from chromatin, or indirectly, by influencing TF abundance or localization.

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          PDSM, a motif for phosphorylation-dependent SUMO modification.

          Ville Hietakangas, Julius Anckar, Henri Blomster … (2006)
          SUMO (small ubiquitin-like modifier) modification regulates many cellular processes, including transcription. Although sumoylation often occurs on specific lysines within the consensus tetrapeptide PsiKxE, other modifications, such as phosphorylation, may regulate the sumoylation of a substrate. We have discovered PDSM (phosphorylation-dependent sumoylation motif), composed of a SUMO consensus site and an adjacent proline-directed phosphorylation site (PsiKxExxSP). The highly conserved motif regulates phosphorylation-dependent sumoylation of multiple substrates, such as heat-shock factors (HSFs), GATA-1, and myocyte enhancer factor 2. In fact, the majority of the PDSM-containing proteins are transcriptional regulators. Within the HSF family, PDSM is conserved between two functionally distinct members, HSF1 and HSF4b, whose transactivation capacities are repressed through the phosphorylation-dependent sumoylation. As the first recurrent sumoylation determinant beyond the consensus tetrapeptide, the PDSM provides a valuable tool in predicting new SUMO substrates.
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            SUMO-targeted ubiquitin ligases.

            R. Jürgen Dohmen, Annie M Sriramachandran (2013)
            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. © 2013. Published by Elsevier B.V. All rights reserved.
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              Sumoylation at chromatin governs coordinated repression of a transcriptional program essential for cell growth and proliferation

              Hélène Neyret‐Kahn, Moussa Benhamed, Tao Ye … (2013)
              Despite numerous studies on specific sumoylated transcriptional regulators, the global role of SUMO on chromatin in relation to transcription regulation remains largely unknown. Here, we determined the genome-wide localization of SUMO1 and SUMO2/3, as well as of UBC9 (encoded by UBE2I) and PIASY (encoded by PIAS4), two markers for active sumoylation, along with Pol II and histone marks in proliferating versus senescent human fibroblasts together with gene expression profiling. We found that, whereas SUMO alone is widely distributed over the genome with strong association at active promoters, active sumoylation occurs most prominently at promoters of histone and protein biogenesis genes, as well as Pol I rRNAs and Pol III tRNAs. Remarkably, these four classes of genes are up-regulated by inhibition of sumoylation, indicating that SUMO normally acts to restrain their expression. In line with this finding, sumoylation-deficient cells show an increase in both cell size and global protein levels. Strikingly, we found that in senescent cells, the SUMO machinery is selectively retained at histone and tRNA gene clusters, whereas it is massively released from all other unique chromatin regions. These data, which reveal the highly dynamic nature of the SUMO landscape, suggest that maintenance of a repressive environment at histone and tRNA loci is a hallmark of the senescent state. The approach taken in our study thus permitted the identification of a common biological output and uncovered hitherto unknown functions for active sumoylation at chromatin as a key mechanism that, in dynamically marking chromatin by a simple modifier, orchestrates concerted transcriptional regulation of a network of genes essential for cell growth and proliferation.
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                Author and article information

                Journal
                Journal ID (nlm-ta): Transcription
                Journal ID (iso-abbrev): Transcription
                Journal ID (publisher-id): KTRN
                Journal ID (publisher-id): ktrn20
                Title: Transcription
                Publisher: Taylor & Francis
                ISSN (Print): 2154-1264
                ISSN (Electronic): 2154-1272
                Publication date Collection: 2017
                Publication date (Electronic): 5 April 2017
                Publication date PMC-release: 5 April 2017
                Volume: 8
                Issue: 4
                Pages: 220-231
                Affiliations
                Department of Biology, York University , Toronto, ON, Canada
                Author notes
                CONTACT Emanuel Rosonina rosonina@ 123456yorku.ca Department of Biology, York University , 4700 Keele St., Toronto, ON, M3J 1P3, Canada

                Color versions of one or more of the figures in the article can be found online at www.tandfonline.com/ktrn.

                [†]

                These authors contributed equally.

                Author information
                https://orcid.org/0000-0001-6861-3143
                https://orcid.org/0000-0001-6157-2211
                Article
                Publisher ID: 1311829
                DOI: 10.1080/21541264.2017.1311829
                PMC ID: 5574528
                PubMed ID: 28379052
                SO-VID: 99291827-22cb-4cae-bd81-23d0302679d6
                Copyright © © 2017 The Author(s). Published with license by Taylor & Francis
                License:

                This is an Open Access article distributed under the terms of the Creative Commons Attribution-NonCommercial-NoDerivatives License ( http://creativecommons.org/licenses/by-nc-nd/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited, and is not altered, transformed, or built upon in any way.

                History
                Date received : 13 February 2017
                Date revision received : 21 March 2017
                Date accepted : 22 March 2017
                Page count
                Figures: 2, Tables: 1, Equations: 0, References: 80, Pages: 12
                Categories
                Subject: Review

                ScienceOpen disciplines: Molecular biology
                Keywords: activator,repressor,sumo,sumoylation,transcription,transcription factor
                Data availability:
                ScienceOpen disciplines: Molecular biology
                Keywords: activator, repressor, sumo, sumoylation, transcription, transcription factor

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