ArticleCellular microbiology2012
Activation of a plant nucleotide binding-leucine rich repeat disease resistance protein by a modified self protein.
Article in Cellular microbiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 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.
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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
40 citing papers in PubMed, 85 citations in OpenAlex.
- An Apple Susceptibility-Related LRR Receptor-Like Kinase MdRLKT21 Activates Plant Immunity by Hijacking a Trans-Kingdom Fungal microRNA-Like RNA.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- The resistance awakens: Diversity at the DNA, RNA, and protein levels informs engineering of plant immune receptors from Arabidopsis to crops.The Plant cell · 2025Review
- Pattern-Triggered Immunity and Effector-Triggered Immunity: crosstalk and cooperation of PRR and NLR-mediated plant defense pathways during host-pathogen interactions.Physiology and molecular biology of plants : an international journal of functional plant biology · 2024Review
- Evolutionary trajectory of pattern recognition receptors in plants.Nature communications · 2024Article
- Altering Specificity and Autoactivity of Plant Immune Receptors Sr33 and Sr50 Via a Rational Engineering Approach.Molecular plant-microbe interactions : MPMI · 2023Article
- Structural mechanism of heavy metal-associated integrated domain engineering of paired nucleotide-binding and leucine-rich repeat proteins in rice.Frontiers in plant science · 2023Review
- Engineering plant immune circuit: walking to the bright future with a novel toolbox.Plant biotechnology journal · 2023Review
- Effector-triggered inhibition of nodulation: A rhizobial effector protease targets soybean kinase GmPBS1-1.Plant physiology · 2022Article
- Decoy engineering of the receptor-like cytoplasmic kinase StPBS1 to defend against virus infection in potato.Molecular plant pathology · 2022Article
- Thirty years of resistance: Zig-zag through the plant immune system.The Plant cell · 2022Review
- ZAR1: Guardian of plant kinases.Frontiers in plant science · 2022Review
- An Ancestry Perspective of the Evolution of PBS1 Proteins in Plants.International journal of molecular sciences · 2021Article
- What the Wild Things Do: Mechanisms of Plant Host Manipulation by Bacterial Type III-Secreted Effector Proteins.Microorganisms · 2021Review
- Recent Advances in Effector-Triggered Immunity in Plants: New Pieces in the Puzzle Create a Different Paradigm.International journal of molecular sciences · 2021Review
- Nuclear Localization of HopA1Plants (Basel, Switzerland) · 2021Article
- Advancement of research on plant NLRs evolution, biochemical activity, structural association, and engineering.Planta · 2020Review
- Transcriptome analysis of Eucalyptus grandis genotypes reveals constitutive overexpression of genes related to rust (Austropuccinia psidii) resistance.Plant molecular biology · 2020Article
- Cross Kingdom Immunity: The Role of Immune Receptors and Downstream Signaling in Animal and Plant Cell Death.Frontiers in immunology · 2020Review
- Development of a Multiparent Population for Genetic Mapping and Allele Discovery in Six-Row Barley.Genetics · 2019Article
- Perturbations of the ZED1 pseudokinase activate plant immunity.PLoS pathogens · 2019Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Nucleotide binding-leucine rich repeat (NB-LRR) proteins function as intracellular receptors for the detection of pathogens in both plants and animals. Despite their central role in innate immunity, the molecular mechanisms that govern NB-LRR activation are poorly understood. The Arabidopsis NB-LRR protein RPS5 detects the presence of the Pseudomonas syringae effector protein AvrPphB by monitoring the status of the Arabidopsis protein kinase PBS1. AvrPphB is a cysteine protease that targets PBS1 for cleavage at a single site within the activation loop of PBS1. Using a transient expression system in the plant Nicotiana benthamiana and stable transgenic Arabidopsis plants we found that both PBS1 cleavage products are required to activate RPS5 and can do so in the absence of AvrPphB. We also found, however, that the requirement for cleavage of PBS1 could be bypassed simply by inserting five amino acids at the PBS1 cleavage site, which is located at the apex of the activation loop of PBS1. Activation of RPS5 did not require PBS1 kinase function, and thus RPS5 appears to sense a subtle conformational change in PBS1, rather than cleavage. This finding suggests that NB-LRR proteins may function as fine-tuned sensors of alterations in the structures of effector targets.
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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.