SUMO Chains Rule on Chromatin Occupancy
The dynamic and reversible post-translational modification of proteins and protein complexes with the ubiquitin-related SUMO modifier regulates a wide variety of nuclear functions, such as transcription, replication and DNA repair. SUMO can be attached as a monomer to its targets, but can also form...
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| Format: | Article |
| Language: | English |
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Frontiers Media S.A.
2020-01-01
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| Series: | Frontiers in Cell and Developmental Biology |
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| Online Access: | https://www.frontiersin.org/article/10.3389/fcell.2019.00343/full |
| _version_ | 1828492762282983424 |
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| author | Jan Keiten-Schmitz Kathrin Schunck Stefan Müller |
| author_facet | Jan Keiten-Schmitz Kathrin Schunck Stefan Müller |
| author_sort | Jan Keiten-Schmitz |
| collection | DOAJ |
| description | The dynamic and reversible post-translational modification of proteins and protein complexes with the ubiquitin-related SUMO modifier regulates a wide variety of nuclear functions, such as transcription, replication and DNA repair. SUMO can be attached as a monomer to its targets, but can also form polymeric SUMO chains. While monoSUMOylation is generally involved in the assembly of protein complexes, multi- or polySUMOylation may have very different consequences. The evolutionary conserved paradigmatic signaling process initiated by multi- or polySUMOylation is the SUMO-targeted Ubiquitin ligase (StUbL) pathway, where the presence of multiple SUMO moieties primes ubiquitylation by the mammalian E3 ubiquitin ligases RNF4 or RNF111, or the yeast Slx5/8 heterodimer. The mammalian SUMO chain-specific isopeptidases SENP6 or SENP7, or yeast Ulp2, counterbalance chain formation thereby limiting StUbL activity. Many facets of SUMO chain signaling are still incompletely understood, mainly because only a limited number of polySUMOylated substrates have been identified. Here we summarize recent work that revealed a highly interconnected network of candidate polySUMO modified proteins functioning in DNA damage response and chromatin organization. Based on these datasets and published work on distinct polySUMO-regulated processes we discuss overarching concepts in SUMO chain function. We propose an evolutionary conserved role of polySUMOylation in orchestrating chromatin dynamics and genome stability networks by balancing chromatin-residency of protein complexes. This concept will be exemplified in processes, such as centromere/kinetochore organization, sister chromatid cohesion, DNA repair and replication. |
| first_indexed | 2024-12-11T11:26:09Z |
| format | Article |
| id | doaj.art-4a7a2b8da90c45c8b5912f81b5aac158 |
| institution | Directory Open Access Journal |
| issn | 2296-634X |
| language | English |
| last_indexed | 2024-12-11T11:26:09Z |
| publishDate | 2020-01-01 |
| publisher | Frontiers Media S.A. |
| record_format | Article |
| series | Frontiers in Cell and Developmental Biology |
| spelling | doaj.art-4a7a2b8da90c45c8b5912f81b5aac1582022-12-22T01:09:00ZengFrontiers Media S.A.Frontiers in Cell and Developmental Biology2296-634X2020-01-01710.3389/fcell.2019.00343509749SUMO Chains Rule on Chromatin OccupancyJan Keiten-SchmitzKathrin SchunckStefan MüllerThe dynamic and reversible post-translational modification of proteins and protein complexes with the ubiquitin-related SUMO modifier regulates a wide variety of nuclear functions, such as transcription, replication and DNA repair. SUMO can be attached as a monomer to its targets, but can also form polymeric SUMO chains. While monoSUMOylation is generally involved in the assembly of protein complexes, multi- or polySUMOylation may have very different consequences. The evolutionary conserved paradigmatic signaling process initiated by multi- or polySUMOylation is the SUMO-targeted Ubiquitin ligase (StUbL) pathway, where the presence of multiple SUMO moieties primes ubiquitylation by the mammalian E3 ubiquitin ligases RNF4 or RNF111, or the yeast Slx5/8 heterodimer. The mammalian SUMO chain-specific isopeptidases SENP6 or SENP7, or yeast Ulp2, counterbalance chain formation thereby limiting StUbL activity. Many facets of SUMO chain signaling are still incompletely understood, mainly because only a limited number of polySUMOylated substrates have been identified. Here we summarize recent work that revealed a highly interconnected network of candidate polySUMO modified proteins functioning in DNA damage response and chromatin organization. Based on these datasets and published work on distinct polySUMO-regulated processes we discuss overarching concepts in SUMO chain function. We propose an evolutionary conserved role of polySUMOylation in orchestrating chromatin dynamics and genome stability networks by balancing chromatin-residency of protein complexes. This concept will be exemplified in processes, such as centromere/kinetochore organization, sister chromatid cohesion, DNA repair and replication.https://www.frontiersin.org/article/10.3389/fcell.2019.00343/fullRNF4StUbLSENP6PolySUMOylationSUMO chains |
| spellingShingle | Jan Keiten-Schmitz Kathrin Schunck Stefan Müller SUMO Chains Rule on Chromatin Occupancy Frontiers in Cell and Developmental Biology RNF4 StUbL SENP6 PolySUMOylation SUMO chains |
| title | SUMO Chains Rule on Chromatin Occupancy |
| title_full | SUMO Chains Rule on Chromatin Occupancy |
| title_fullStr | SUMO Chains Rule on Chromatin Occupancy |
| title_full_unstemmed | SUMO Chains Rule on Chromatin Occupancy |
| title_short | SUMO Chains Rule on Chromatin Occupancy |
| title_sort | sumo chains rule on chromatin occupancy |
| topic | RNF4 StUbL SENP6 PolySUMOylation SUMO chains |
| url | https://www.frontiersin.org/article/10.3389/fcell.2019.00343/full |
| work_keys_str_mv | AT jankeitenschmitz sumochainsruleonchromatinoccupancy AT kathrinschunck sumochainsruleonchromatinoccupancy AT stefanmuller sumochainsruleonchromatinoccupancy |