ArticleProceedings of the National Academy of Sciences of the United States of America2010
Proteome-wide screens for small ubiquitin-like modifier (SUMO) substrates identify Arabidopsis proteins implicated in diverse biological processes.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 99 papers.
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Who cites it
99 citing papers in PubMed, 168 citations in OpenAlex.
- Nitrate-induced NLP1 SUMOylation regulates nitrate signaling and root nodulation.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Genome-wide identification and expression analysis of the Small Ubiquitin-like Modifier (SUMO) gene family in Triticum aestivum L.BMC genomics · 2025Article
- SUMOylation of BAK1 regulates its co-receptor function for specifically activating brassinosteroid response.Plant communications · 2025Article
- Elucidating tissue and subcellular specificity of the entire SUMO network reveals how stress responses are fine-tuned in a eukaryote.Science advances · 2025Article
- Multifaceted roles of SUMO in DNA metabolism.Nucleus (Austin, Tex.) · 2024Review
- Highly sensitive site-specific SUMOylation proteomics in Arabidopsis.Nature plants · 2024Article
- Gene pyramiding for boosted plant growth and broad abiotic stress tolerance.Plant biotechnology journal · 2024Article
- NUA positively regulates plant immunity by coordination with ESD4 to deSUMOylate TPR1 in Arabidopsis.The New phytologist · 2024Article
- A robust method for identification of plant SUMOylation substrates in a library-based reconstitution system.Plant communications · 2023Article
- A plant RNA virus inhibits NPR1 sumoylation and subverts NPR1-mediated plant immunity.Nature communications · 2023Article
- Bioinformatic Tools for Exploring the SUMO Gene Network: An Update.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Regulatory Network of Serine/Arginine-Rich (SR) Proteins: The Molecular Mechanism and Physiological Function in Plants.International journal of molecular sciences · 2022Review
- SUMO E3 ligase SIZ1 connects sumoylation and reactive oxygen species homeostasis processes in Arabidopsis.Plant physiology · 2022Article
- Fine-tuning of SUMOylation modulates drought tolerance of apple.Plant biotechnology journal · 2022Article
- Review
- Root responses to aluminium and iron stresses require the SIZ1 SUMO ligase to modulate the STOP1 transcription factor.The Plant journal : for cell and molecular biology · 2021Article
- The converging path of protein SUMOylation in phytohormone signalling: highlights and new frontiers.Plant cell reports · 2021Review
- Phototropin Interactions with SUMO Proteins.Plant & cell physiology · 2021Article
- Article
- SUMO Modification of OsFKBP20-1b Is Integral to Proper Pre-mRNA Splicing upon Heat Stress in Rice.International journal of molecular sciences · 2021Article
39 more citing papers are in PubMed but not listed here.
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Covalent modification of proteins by small ubiquitin-like modifier (SUMO) regulates various cellular activities in yeast and mammalian cells. In Arabidopsis, inactivation of genes encoding SUMO or SUMO-conjugation enzymes is lethal, emphasizing the importance of SUMOylation in plant development. Despite this, little is known about SUMO targets in plants. Here we identified 238 Arabidopsis proteins as potential SUMO substrates because they interacted with SUMO-conjugating enzyme and/or SUMO protease (ESD4) in the yeast two-hybrid system. Compared with the whole Arabidopsis proteome, the identified proteins were strongly enriched for those containing high-probability consensus SUMO attachment sites, further supporting that they are true SUMO substrates. A high-throughput assay was developed in Escherichia coli and used to test the SUMOylation of 56% of these proteins. More than 92% of the proteins tested were SUMOylated in this assay by at least one SUMO isoform. Furthermore, ADA2b, an ESD4 interactor that was SUMOylated in the E. coli system, also was shown to be SUMOylated in Arabidopsis. The identified SUMO substrates are involved in a wide range of plant processes, many of which were not previously known to involve SUMOylation. These proteins provide a basis for exploring the function of SUMOylation in the regulation of diverse processes in Arabidopsis.
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