ArticlePLoS pathogens2017
Protein-protein interactions in the RPS4/RRS1 immune receptor complex.
Article in PLoS pathogens, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers, 1 of them a synthesis that pooled it.
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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.
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Who cites it
52 citing papers in PubMed, 1 synthesis or guideline pooled it, 134 citations in OpenAlex.
- Interactomics in plant defence: progress and opportunities.Molecular biology reports · 2023Pooled it
- Review
- Transition metal-enhanced immunity in Arabidopsis roots via an NLR pair.Nature plants · 2026Article
- The Landscape of Integrated Domains of Angiosperm NLR Genes Reveals Continuous Architecture Evolution of Plant Intracellular Immune Receptors.Plants (Basel, Switzerland) · 2025Article
- The pan-NLRome and diversity of Watkins wheat provide genetic resources for improving disease resistance and adaptation.Plant communications · 2025Article
- Two complementary NLRs from wild emmer wheat confer powdery mildew resistance.Nature communications · 2025Article
- TheProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Interaction of Potato Autophagy-Related StATG8 Family Proteins with Pathogen Effector and WRKY Transcription Factor in the Nucleus.Microorganisms · 2025Article
- A root-specific NLR network mediates immune signaling of resistance genes against plant parasitic nematodes.The Plant cell · 2025Article
- A head-to-head NLR gene pair from wild emmer confers stripe rust resistance in wheat.Nature genetics · 2025Article
- Reversible ubiquitination conferred by domain shuffling controls paired NLR immune receptor complex homeostasis in plant immunity.Nature communications · 2025Article
- A KNOX Ⅱ transcription factor suppresses the NLR immune receptor BRG8-mediated immunity in rice.Plant communications · 2024Article
- An pair of an atypical NLR encoding genes confer Asian soybean rust resistance in soybean.Nature communications · 2024Article
- Bacterial host adaptation through sequence and structural variations of a single type III effector gene.iScience · 2024Article
- Paired plant immune CHS3-CSA1 receptor alleles form distinct hetero-oligomeric complexes.Science (New York, N.Y.) · 2024Article
- Article
- The melonPlant direct · 2024Article
- NLR receptors in plant immunity: making sense of the alphabet soup.EMBO reports · 2023Review
- NLR immune receptors: structure and function in plant disease resistance.Biochemical Society transactions · 2023Review
- Mutagenesis of the melon Prv gene by CRISPR/Cas9 breaks papaya ringspot virus resistance and generates an autoimmune allele with constitutive defense responses.Journal of experimental botany · 2023Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
Plant NLR (Nucleotide-binding domain and Leucine-rich Repeat) immune receptor proteins are encoded by Resistance (R) genes and confer specific resistance to pathogen races that carry the corresponding recognized effectors. Some NLR proteins function in pairs, forming receptor complexes for the perception of specific effectors. We show here that the Arabidopsis RPS4 and RRS1 NLR proteins are both required to make an authentic immune complex. Over-expression of RPS4 in tobacco or in Arabidopsis results in constitutive defense activation; this phenotype is suppressed in the presence of RRS1. RRS1 protein co-immunoprecipitates (co-IPs) with itself in the presence or absence of RPS4, but in contrast, RPS4 does not associate with itself in the absence of RRS1. In the presence of RRS1, RPS4 associates with defense signaling regulator EDS1 solely in the nucleus, in contrast to the extra-nuclear location found in the absence of RRS1. The AvrRps4 effector does not disrupt RPS4-EDS1 association in the presence of RRS1. In the absence of RRS1, AvrRps4 interacts with EDS1, forming nucleocytoplasmic aggregates, the formation of which is disturbed by the co-expression of PAD4 but not by SAG101. These data indicate that the study of an immune receptor protein complex in the absence of all components can result in misleading inferences, and reveals an NLR complex that dynamically interacts with the immune regulators EDS1/PAD4 or EDS1/SAG101, and with effectors, during the process by which effector recognition is converted to defense activation.
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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.