ArticlePLoS computational biology2010
A mechanistic view of the role of E3 in sumoylation.
Article in PLoS computational biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed.
- Viral RNA polymerase as a SUMOylation decoy inhibits RNA quality control to promote potyvirus infection.Nature communications · 2025Article
- The SUMO Family: Mechanisms and Implications in Thyroid Cancer Pathogenesis and Therapy.Biomedicines · 2024Review
- SUMO/deSUMOylation of the BRI1 brassinosteroid receptor modulates plant growth responses to temperature.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- The Role of SUMO E3 Ligases in Signaling Pathway of Cancer Cells.International journal of molecular sciences · 2022Review
- Article
- Proteomic Approaches to Dissect Host SUMOylation during Innate Antiviral Immune Responses.Viruses · 2021Review
- Current Status of SUMOylation Inhibitors.Current medicinal chemistry · 2021Review
- Casein kinase-2-mediated phosphorylation increases the SUMO-dependent activity of the cytomegalovirus transactivator IE2.The Journal of biological chemistry · 2019Article
- SUMO conjugation to the pattern recognition receptor FLS2 triggers intracellular signalling in plant innate immunity.Nature communications · 2018Article
- Active Site Gate Dynamics Modulate the Catalytic Activity of the Ubiquitination Enzyme E2-25K.Scientific reports · 2018Article
- Chemical shift perturbation mapping of the Ubc9-CRMP2 interface identifies a pocket in CRMP2 amenable for allosteric modulation of Nav1.7 channels.Channels (Austin, Tex.) · 2018Article
- Advances in the development of SUMO specific protease (SENP) inhibitors.Computational and structural biotechnology journal · 2015Review
- SUMOylation by the E3 ligase TbSIZ1/PIAS1 positively regulates VSG expression in Trypanosoma brucei.PLoS pathogens · 2014Article
- Multiple conformational selection and induced fit events take place in allosteric propagation.Biophysical chemistry · 2014Review
- Conformational control of the binding of the transactivation domain of the MLL protein and c-Myb to the KIX domain of CREB.PLoS computational biology · 2012Article
- Loop 7 of E2 enzymes: an ancestral conserved functional motif involved in the E2-mediated steps of the ubiquitination cascade.PloS one · 2012Article
- Entropy-driven mechanism of an E3 ligase.Biochemistry · 2011Article
- Alternative allosteric mechanisms can regulate the substrate and E2 in SUMO conjugation.Journal of molecular biology · 2011Article
- The role of allostery in the ubiquitin-proteasome system.Critical reviews in biochemistry and molecular biologyReview
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4 authors.
Funding
Abstract
Sumoylation, the covalent attachment of SUMO (Small Ubiquitin-Like Modifier) to proteins, differs from other Ubl (Ubiquitin-like) pathways. In sumoylation, E2 ligase Ubc9 can function without E3 enzymes, albeit with lower reaction efficiency. Here, we study the mechanism through which E3 ligase RanBP2 triggers target recognition and catalysis by E2 Ubc9. Two mechanisms were proposed for sumoylation. While in both the first step involves Ubc9 conjugation to SUMO, the subsequent sequence of events differs: in the first E2-SUMO forms a complex with the target and E3, followed by SUMO transfer to the target. In the second, Ubc9-SUMO binds to the target and facilitates SUMO transfer without E3. Using dynamic correlations obtained from explicit solvent molecular dynamic simulations we illustrate the key roles played by allostery in both mechanisms. Pre-existence of conformational states explains the experimental observations that sumoylation can occur without E3, even though at a reduced rate. Furthermore, we propose a mechanism for enhancement of sumoylation by E3. Analysis of the conformational ensembles of the complex of E2 conjugated to SUMO illustrates that the E2 enzyme is already largely pre-organized for target binding and catalysis; E3 binding shifts the equilibrium and enhances these pre-existing populations. We further observe that E3 binding regulates allosterically the key residues in E2, Ubc9 Asp100/Lys101 E2, for the target recognition.
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