ArticleNature plants2024
Highly sensitive site-specific SUMOylation proteomics in Arabidopsis.
Article in Nature plants, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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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.
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Who cites it
9 citing papers in PubMed.
- SUMOylation: an emerging field of protein modification in horticultural plants.Horticulture research · 2026Review
- In Vivo and In Vitro SUMOylation Assays inBio-protocol · 2026Article
- SUMOylation in plants: A versatile post-translational mechanism responding to environmental stresses.Journal of integrative plant biology · 2026Review
- SIZ1-mediated SUMOylation of HAT1 enhances plant thermotolerance in Arabidopsis.The Plant journal : for cell and molecular biology · 2026Article
- Elucidating tissue and subcellular specificity of the entire SUMO network reveals how stress responses are fine-tuned in a eukaryote.Science advances · 2025Article
- Review
- Integrated Single-Tip IMAC-HILIC Enables Simultaneous Analysis of Plant Phosphoproteomics and N-Glycoproteomics.Journal of proteome research · 2025Article
- Recent advances in proteomic workflows to interrogate the SUMOylome in plants.The New phytologist · 2025Review
- MYC2-SUMO protease feedback loops boost salt tolerance in wheat.The New phytologist · 2025Article
Corrections and comments
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
SUMOylation-the attachment of a small ubiquitin-like modifier (SUMO) to target proteins-plays roles in controlling plant growth, nutrient signalling and stress responses. SUMOylation studies in plants are scarce because identifying SUMOylated proteins and their sites is challenging. To date, only around 80 SUMOylation sites have been identified. Here we introduce lysine-null SUMO1 into the Arabidopsis sumo1 sumo2 mutant and establish a two-step lysine-null SUMO enrichment method. We identified a site-specific SUMOylome comprising over 2,200 SUMOylation sites from 1,300 putative acceptors that function in numerous nuclear processes. SUMOylation marks occur on several motifs, differing from the canonical ψKxE motif in distant eukaryotes. Quantitative comparisons demonstrate that SUMOylation predominantly enhances the stability of SUMO1 acceptors. Our study delivers a highly sensitive and efficient method for site-specific SUMOylome studies and provides a comprehensive catalogue of Arabidopsis SUMOylation, serving as a valuable resource with which to further explore how SUMOylation regulates protein function.
Indexed as
Identifiers
39294263What Socratic 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 Socratic graph.