ArticleScientific reports2017
Structural analysis and evolution of specificity of the SUMO UFD E1-E2 interactions.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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Who cites it
6 citing papers in PubMed.
- (De)Activation (Ir)Reversibly or Degradation: Dynamics of Post-Translational Protein Modifications in Plants.Life (Basel, Switzerland) · 2022Review
- 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
- SUMOylation in Phytopathogen Interactions: Balancing Invasion and Resistance.Frontiers in cell and developmental biology · 2021Review
- Not So Slim Anymore-Evidence for the Role of SUMO in the Regulation of Lipid Metabolism.Biomolecules · 2020Review
- Insights into the transcriptional and post-transcriptional regulation of the rice SUMOylation machinery and into the role of two rice SUMO proteases.BMC plant biology · 2018Article
- SUMO chain formation relies on the amino-terminal region of SUMO-conjugating enzyme and has dedicated substrates in plants.The Biochemical journal · 2018Article
Corrections and comments
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Authors and funding
3 authors.
Funding
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Abstract
SUMO belongs to the ubiquitin-like family (UbL) of protein modifiers. SUMO is conserved among eukaryotes and is essential for the regulation of processes such as DNA damage repair, transcription, DNA replication and mitosis. UbL modification of proteins occurs via a specific enzymatic cascade formed by the crosstalk between the E1-activating enzyme, the E2-conjugating enzyme and the E3-ligase. An essential discrimination step in all UbL modifiers corresponds to the interaction between E1 and E2 enzymes, which is mediated by the recruitment of the E2 to the UFD domain (Ubiquitin-Fold Domain) of the E1 enzyme. To gain insights in the properties of this interface, we have compared the structures of the complexes between E1 UFD domain and E2 in human and yeast, revealing two alternative UFD platforms that interact with a conserved E2. Comparative sequence analysis of the E1 UFD domain indicates that the E2 binding region has been conserved across phylogenetic closely related species, in which higher sequence conservation can be found in the E2 binding region than in the entire UFD domain. These distinctive strategies for E1-E2 interactions through the UFD domain might be the consequence of a high selective pressure to ensure specificity of each modifier conjugation system.
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