ArticlePloS one2010
Crystal structure of UBA2(ufd)-Ubc9: insights into E1-E2 interactions in Sumo pathways.
Article in PloS one, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 51 citations in OpenAlex.
- UBA2: the gatekeeper of the sumoylation pathway and its multifaceted roles in human diseases and therapeutic prospects.Clinical and experimental medicine · 2026Review
- UBA6 specificity for ubiquitin E2 conjugating enzymes reveals a priority mechanism of BIRC6.Nature structural & molecular biology · 2026Article
- Cryo-EM structures reveal the molecular mechanism of SUMO E1-E2 thioester transfer.Nature structural & molecular biology · 2025Article
- Molecular choreography of E1 enzymes in ubiquitin-like protein cascades: New insights into dynamics and specificity.The Journal of biological chemistry · 2025Review
- The SUMO Family: Mechanisms and Implications in Thyroid Cancer Pathogenesis and Therapy.Biomedicines · 2024Review
- SUMOylation of Warts kinase promotes neural stem cell reactivation.Nature communications · 2024Article
- Review
- The B-box1 domain of PML mediates SUMO E2-E3 complex formation through an atypical interaction with UBC9.Biophysical chemistry · 2022Article
- SUMO conjugating enzyme: a vital player of SUMO pathway in plants.Physiology and molecular biology of plants : an international journal of functional plant biology · 2021Review
- SUMO mediated regulation of transcription factors as a mechanism for transducing environmental cues into cellular signaling in plants.Cellular and molecular life sciences : CMLS · 2021Review
- Review
- The in vivo ISGylome links ISG15 to metabolic pathways and autophagy upon Listeria monocytogenes infection.Nature communications · 2019Article
- Structural basis for the nuclear import and export functions of the biportin Pdr6/Kap122.The Journal of cell biology · 2019Article
- Molecular mechanism of a covalent allosteric inhibitor of SUMO E1 activating enzyme.Nature communications · 2018Article
- Ubiquitin-like Protein Conjugation: Structures, Chemistry, and Mechanism.Chemical reviews · 2018Review
- Molecular mechanism of K65 acetylation-induced attenuation of Ubc9 and the NDSM interaction.Scientific reports · 2017Article
- Site-specific inhibition of the small ubiquitin-like modifier (SUMO)-conjugating enzyme Ubc9 selectively impairs SUMO chain formation.The Journal of biological chemistry · 2017Article
- Structural analysis and evolution of specificity of the SUMO UFD E1-E2 interactions.Scientific reports · 2017Article
- Insights Into the Allosteric Inhibition of the SUMO E2 Enzyme Ubc9.Angewandte Chemie (International ed. in English) · 2016Article
- Characterization and Structural Insights into Selective E1-E2 Interactions in the Human and Plasmodium falciparum SUMO Conjugation Systems.The Journal of biological chemistry · 2016Article
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
Canonical ubiquitin-like proteins (UBLs) such as ubiquitin, Sumo, NEDD8, and ISG15 are ligated to targets by E1-E2-E3 multienzyme cascades. The Sumo cascade, conserved among all eukaryotes, regulates numerous biological processes including protein localization, transcription, DNA replication, and mitosis. Sumo conjugation is initiated by the heterodimeric Aos1-Uba2 E1 enzyme (in humans called Sae1-Uba2), which activates Sumo's C-terminus, binds the dedicated E2 enzyme Ubc9, and promotes Sumo C-terminal transfer between the Uba2 and Ubc9 catalytic cysteines. To gain insights into details of E1-E2 interactions in the Sumo pathway, we determined crystal structures of the C-terminal ubiquitin fold domain (ufd) from yeast Uba2 (Uba2(ufd)), alone and in complex with Ubc9. The overall structures of both yeast Uba2(ufd) and Ubc9 superimpose well on their individual human counterparts, suggesting conservation of fundamental features of Sumo conjugation. Docking the Uba2(ufd)-Ubc9 and prior full-length human Uba2 structures allows generation of models for steps in Sumo transfer from Uba2 to Ubc9, and supports the notion that Uba2 undergoes remarkable conformational changes during the reaction. Comparisons to previous structures from the NEDD8 cascade demonstrate that UBL cascades generally utilize some parallel E1-E2 interaction surfaces. In addition, the structure of the Uba2(ufd)-Ubc9 complex reveals interactions unique to Sumo E1 and E2. Comparison with a previous Ubc9-E3 complex structure demonstrates overlap between Uba2 and E3 binding sites on Ubc9, indicating that loading with Sumo and E3-catalyzed transfer to substrates are strictly separate steps. The results suggest mechanisms establishing specificity and order in Sumo conjugation cascades.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.