ArticleThe Biochemical journal2011
Distinctive properties of Arabidopsis SUMO paralogues support the in vivo predominant role of AtSUMO1/2 isoforms.
Article in The Biochemical journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
22 citing papers in PubMed.
- The C-terminal SUMOylation-dependent regulation of αKNL2 governs its centromere targeting and interaction with CENH3.Plant communications · 2026Article
- Elucidating tissue and subcellular specificity of the entire SUMO network reveals how stress responses are fine-tuned in a eukaryote.Science advances · 2025Article
- Identification and characterization of novelPeerJ · 2025Article
- Definition and regulatory analysis of the SUMOylation system in Caixin (Brassica rapa var. Parachinensis) during pectobacterium carotovorum infection.BMC plant biology · 2024Article
- Kinetic Analysis of Plant SUMO Conjugation Machinery.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Understanding SUMO-mediated adaptive responses in plants to improve crop productivity.Essays in biochemistry · 2022Review
- SUMO E3 ligase SIZ1 connects sumoylation and reactive oxygen species homeostasis processes in Arabidopsis.Plant physiology · 2022Article
- (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
- 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
- SUMOylation in Phytopathogen Interactions: Balancing Invasion and Resistance.Frontiers in cell and developmental biology · 2021Review
- Global SUMOylome Adjustments in Basal Defenses ofFrontiers in cell and developmental biology · 2021Article
- An Insight into the Factors Influencing Specificity of the SUMO System in Plants.Plants (Basel, Switzerland) · 2020Review
- Dealing With Stress: A Review of Plant SUMO Proteases.Frontiers in plant science · 2019Review
- Overexpression of SUMO1 located predominately to euchromatin of dividing cells affects reproductive development in maize.Plant signaling & behavior · 2019Article
- Geminivirus Replication Protein Impairs SUMO Conjugation of Proliferating Cellular Nuclear Antigen at Two Acceptor Sites.Journal of virology · 2018Article
- Sumoylation ofThe Plant cell · 2017Article
- Structural analysis and evolution of specificity of the SUMO UFD E1-E2 interactions.Scientific reports · 2017Article
- Defining the SUMO System in Maize: SUMOylation Is Up-Regulated during Endosperm Development and Rapidly Induced by Stress.Plant physiology · 2016Article
- Whole-genome duplications followed by tandem duplications drive diversification of the protein modifier SUMO in Angiosperms.The New phytologist · 2016Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
Abstract
Protein modification by SUMO (small ubiquitin-related modifier) has emerged as an essential regulatory mechanism in eukaryotes. Even though the molecular mechanisms of SUMO conjugation/deconjugation are conserved, the number of SUMO machinery components and their degree of conservation are specific to each organism. In the present paper, we show data contributing to the notion that the four expressed Arabidopsis SUMO paralogues, AtSUMO1, 2, 3 and 5, have functionally diverged to a higher extent than their human orthologues. We have explored the degree of conservation of these paralogues and found that the surfaces involved in E1-activating enzyme recognition, and E2-conjugating enzyme and SIM (SUMO-interacting motif) non-covalent interactions are well conserved in AtSUMO1/2 isoforms, whereas AtSUMO3 shows a lower degree of conservation, and AtSUMO5 is the most divergent isoform. These differences are functionally relevant, since AtSUMO3 and 5 are deficient in establishing E2 non-covalent interactions, which has not been reported for any naturally occurring SUMO orthologue. In addition, AtSUMO3 is less efficiently conjugated than AtSUMO1/2, and AtSUMO5 shows the lowest conjugation level. A mutagenesis analysis revealed that decreases in conjugation rate and thioester-bond formation are the result of the non-conserved residues involved in E1-activating enzyme recognition that are present in AtSUMO3 and 5. The results of the present study support a role for the E1-activating enzyme in SUMO paralogue discrimination, providing a new mechanism to favour conjugation of the essential AtSUMO1/2 paralogues.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.