ArticleNature communications2020
SUSA2 is an F-box protein required for autoimmunity mediated by paired NLRs SOC3-CHS1 and SOC3-TN2.
Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 28 citations in OpenAlex.
- Ginseng-derived vesicle-like nanoparticles deliver pgi-MIR6136a-p3 for sepsis therapy via ELF3/NF-κB signaling axis.Journal of nanobiotechnology · 2026Article
- Tuber mustard BjuFIP gene negatively regulates plant sensitivity to abscisic acid.Scientific reports · 2025Article
- Post-Translational Modifications of TOE3 Regulate Antiviral Defense in Tobacco.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Exploring effector candidates in Rhynchosporium commune: insights into their expression dynamics during barley infection.Scientific reports · 2025Article
- TurboID-based proteomic profiling reveals proxitome of ASK1 and CUL1 of the SCF ubiquitin ligase in plants.The New phytologist · 2024Article
- Proteolysis in plant immunity.The Plant cell · 2024Review
- The antagonistic role of an E3 ligase pair in regulating plant NLR-mediated autoimmunity and fungal pathogen resistance.Cell host & microbe · 2024Article
- Molecular innovations in plant TIR-based immunity signaling.The Plant cell · 2022Review
- [Mirror cutting-assisted orthogonal digestion enabling large-scale and accurate protein complex characterization].Se pu = Chinese journal of chromatography · 2022Article
- Plant autoimmunity-fresh insights into an old phenomenon.Plant physiology · 2022Article
- Predication of the Effector Proteins Secreted byJournal of fungi (Basel, Switzerland) · 2022Article
- TheInternational journal of molecular sciences · 2021Article
- A Truncated TIR-NBS Protein TN10 Pairs with Two Clustered TIR-NBS-LRR Immune Receptors and Contributes to Plant Immunity inInternational journal of molecular sciences · 2021Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Both higher plants and mammals rely on nucleotide-binding leucine-rich repeat (NLR) immune receptors to detect pathogens and initiate immunity. Upon effector recognition, plant NLRs oligomerize for defense activation, the mechanism of which is poorly understood. We previously showed that disruption of the E3 ligase, Senescence-Associated E3 Ubiquitin Ligase 1 (SAUL1) leads to the activation of the NLR SOC3. Here, we report the identification of suppressor of saul1 2 (susa2) and susa3 from the saul1-1 suppressor screen. Pairwise interaction analysis suggests that both SUSA proteins interact with components of an SCF
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