ArticlePlant physiology2013
Structural determinants at the interface of the ARC2 and leucine-rich repeat domains control the activation of the plant immune receptors Rx1 and Gpa2.
Article in Plant physiology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.
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48 citing papers in PubMed, 94 citations in OpenAlex.
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- Lessons from Deep Learning Structural Prediction of Multistate Multidomain Proteins-The Case Study of Coiled-Coil NOD-like Receptors.International journal of molecular sciences · 2025Article
- Activation and Autoinhibition Mechanisms of NLR Immune Receptor Pi36 in Rice.International journal of molecular sciences · 2024Article
- An pair of an atypical NLR encoding genes confer Asian soybean rust resistance in soybean.Nature communications · 2024Article
- A dominant-negative avirulence effector of the barley powdery mildew fungus provides mechanistic insight into barley MLA immune receptor activation.Journal of experimental botany · 2023Article
- The Hypersensitive Response to Plant Viruses.Viruses · 2023Review
- Methionine oxidation selectively enhances T cell reactivity against a melanoma antigen.iScience · 2023Article
- Altering Specificity and Autoactivity of Plant Immune Receptors Sr33 and Sr50 Via a Rational Engineering Approach.Molecular plant-microbe interactions : MPMI · 2023Article
- NLRscape: an atlas of plant NLR proteins.Nucleic acids research · 2023Article
- Unmasking the invaders: NLR-mal function in plant defense.Frontiers in plant science · 2023Review
- Structural basis of NLR activation and innate immune signalling in plants.Immunogenetics · 2022Review
- NLRexpress-A bundle of machine learning motif predictors-Reveals motif stability underlying plant Nod-like receptors diversity.Frontiers in plant science · 2022Article
- Tsw - A case study on structure-function puzzles in plant NLRs with unusually large LRR domains.Frontiers in plant science · 2022Article
- Molecular and Cellular Mechanisms Involved in Host-Specific Resistance to Cyst Nematodes in Crops.Frontiers in plant science · 2021Review
- Advancement of research on plant NLRs evolution, biochemical activity, structural association, and engineering.Planta · 2020Review
- Diversity, Function and Regulation of Cell Surface and Intracellular Immune Receptors inPlants (Basel, Switzerland) · 2020Review
- Blast resistance gene Pi54 over-expressed in rice to understand its cellular and sub-cellular localization and response to different pathogens.Scientific reports · 2020Article
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Authors and funding
12 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Many plant and animal immune receptors have a modular nucleotide-binding-leucine-rich repeat (NB-LRR) architecture in which a nucleotide-binding switch domain, NB-ARC, is tethered to a LRR sensor domain. The cooperation between the switch and sensor domains, which regulates the activation of these proteins, is poorly understood. Here, we report structural determinants governing the interaction between the NB-ARC and LRR in the highly homologous plant immune receptors Gpa2 and Rx1, which recognize the potato cyst nematode Globodera pallida and Potato virus X, respectively. Systematic shuffling of polymorphic sites between Gpa2 and Rx1 showed that a minimal region in the ARC2 and N-terminal repeats of the LRR domain coordinate the activation state of the protein. We identified two closely spaced amino acid residues in this region of the ARC2 (positions 401 and 403) that distinguish between autoactivation and effector-triggered activation. Furthermore, a highly acidic loop region in the ARC2 domain and basic patches in the N-terminal end of the LRR domain were demonstrated to be required for the physical interaction between the ARC2 and LRR. The NB-ARC and LRR domains dissociate upon effector-dependent activation, and the complementary-charged regions are predicted to mediate a fast reassociation, enabling multiple rounds of activation. Finally, we present a mechanistic model showing how the ARC2, NB, and N-terminal half of the LRR form a clamp, which regulates the dissociation and reassociation of the switch and sensor domains in NB-LRR proteins.
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