ArticleThe Plant cell2010
Nucleocytoplasmic distribution is required for activation of resistance by the potato NB-LRR receptor Rx1 and is balanced by its functional domains.
Article in The Plant cell, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 91 papers.
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Who cites it
91 citing papers in PubMed.
- Dissection of Cell Death Induction byLife (Basel, Switzerland) · 2026Article
- Virus-Inducible Activation of Hypersensitive Response Confers Broad-Spectrum Resistance to Diverse Viruses in Plants.Molecular plant pathology · 2025Article
- COP9 Signalosome's Role in Plant Defense Mechanisms.Plants (Basel, Switzerland) · 2025Review
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- Gpa2 detects the potato cyst nematode effector GpRBP-1 in the cytoplasm but requires a balanced nucleocytoplasmic distribution to trigger cell death.Journal of experimental botany · 2025Article
- A wheat CC-NBS-LRR protein Ym1 confers WYMV resistance by recognizing viral coat protein.Nature communications · 2025Article
- 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
- Identification and Functional Analysis of thePlants (Basel, Switzerland) · 2024Article
- The melonPlant direct · 2024Article
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- NLRscape: an atlas of plant NLR proteins.Nucleic acids research · 2023Article
- Current status, breeding strategies and future prospects for managing chilli leaf curl virus disease and associated begomoviruses in Chilli (Frontiers in plant science · 2023Review
- Synthetic peptides for the precise transportation of proteins of interests to selectable subcellular areas.Frontiers in bioengineering and biotechnology · 2023Article
- GLYCINE-RICH RNA-BINDING PROTEIN 7 potentiates effector-triggered immunity through an RNA recognition motif.Plant physiology · 2022Article
- Role of the Sw5 Gene Cluster in the Fight against Plant Viruses.Journal of virology · 2022Review
- NLR immune receptor RB is differentially targeted by two homologous but functionally distinct effector proteins.Plant communications · 2021Article
- Perturbation of nuclear-cytosolic shuttling of Rx1 compromises extreme resistance and translational arrest of potato virus X transcripts.The Plant journal : for cell and molecular biology · 2021Article
- Extreme Resistance to Viruses in Potato and Soybean.Frontiers in plant science · 2021Review
- Advancement of research on plant NLRs evolution, biochemical activity, structural association, and engineering.Planta · 2020Review
- UhAVR1, an HR-Triggering Avirulence Effector ofJournal of fungi (Basel, Switzerland) · 2020Article
31 more citing papers are in PubMed but not listed here.
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Authors and funding
14 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Rx1 protein, as many resistance proteins of the nucleotide binding-leucine-rich repeat (NB-LRR) class, is predicted to be cytoplasmic because it lacks discernable nuclear targeting signals. Here, we demonstrate that Rx1, which confers extreme resistance to Potato virus X, is located both in the nucleus and cytoplasm. Manipulating the nucleocytoplasmic distribution of Rx1 or its elicitor revealed that Rx1 is activated in the cytoplasm and cannot be activated in the nucleus. The coiled coil (CC) domain was found to be required for accumulation of Rx1 in the nucleus, whereas the LRR domain promoted the localization in the cytoplasm. Analyses of structural subdomains of the CC domain revealed no autonomous signals responsible for active nuclear import. Fluorescence recovery after photobleaching and nuclear fractionation indicated that the CC domain binds transiently to large complexes in the nucleus. Disruption of the Rx1 resistance function and protein conformation by mutating the ATP binding phosphate binding loop in the NB domain, or by silencing the cochaperone SGT1, impaired the accumulation of Rx1 protein in the nucleus, while Rx1 versions lacking the LRR domain were not affected in this respect. Our results support a model in which interdomain interactions and folding states determine the nucleocytoplasmic distribution of Rx1.
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