ArticleThe Journal of biological chemistry2011
Physical association of Arabidopsis hypersensitive induced reaction proteins (HIRs) with the immune receptor RPS2.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.
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58 citing papers in PubMed, 101 citations in OpenAlex.
- The Arabidopsis SPFH protein HIR2 modulates receptor signaling and plasma membrane organization.The EMBO journal · 2026Article
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- Mechanisms controlling the plasma membrane targeting and the nanodomain organization of the plant SPFH protein HIR2.The Plant journal : for cell and molecular biology · 2026Article
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- Photosystem Perturbation by Staygreen Mutations Confers Allele-Dependent Defences Against Infections of Pathogens With Different Lifestyles and Abiotic Stress Tolerance.Plant, cell & environment · 2026Article
- Transcription factor VlPAT2 enhances the resistance of grapevine to Botrytis cinerea by promoting ROS accumulation.Plant cell reports · 2025Article
- Plasticity of the Arabidopsis leaf lipidome and proteome in response to pathogen infection and heat stress.Plant physiology · 2025Article
- Membrane nanodomains to shape plant cellular functions and signaling.The New phytologist · 2025Review
- An effector essential for virulence of necrotrophic fungi targets plant HIRs to inhibit host immunity.Nature communications · 2024Article
- Arabidopsis apoplast TET8 positively correlates to leaf senescence, andPlant direct · 2024Article
- Genome-wide identification and expression profile ofFrontiers in plant science · 2024Article
- Phased grapevine genome sequence of anFrontiers in plant science · 2023Article
- Transcriptomics Using the Enriched Arabidopsis Shoot Apex Reveals Developmental Priming Genes Involved in Plastic Plant Growth under Salt Stress Conditions.Plants (Basel, Switzerland) · 2022Article
- The apple FERONIA receptor-like kinase MdMRLK2 negatively regulates Valsa canker resistance by suppressing defence responses and hypersensitive reaction.Molecular plant pathology · 2022Article
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- Molecular mechanisms of resistance toFrontiers in plant science · 2022Article
- Environmental Cues Contribute to Dynamic Plasma Membrane Organization of Nanodomains Containing Flotillin-1 and Hypersensitive Induced Reaction-1 Proteins inFrontiers in plant science · 2022Article
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- Telomerase Interaction Partners-Insight from Plants.International journal of molecular sciences · 2021Article
- Membrane nanodomains and transport functions in plant.Plant physiology · 2021Review
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Authors and funding
9 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Arabidopsis RPS2 is a typical nucleotide-binding leucine-rich repeat resistance protein, which indirectly recognizes the bacterial effector protein AvrRpt2 and thereby activates effector-triggered immunity (ETI). Previously, we identified two hypersensitive induced reaction (AtHIR) proteins, AtHIR1 (At1g09840) and AtHIR2 (At3g01290), as potential RPS2 complex components. AtHIR proteins contain the stomatin/prohibitin/flotillin/HflK/C domain (also known as the prohibitin domain or band 7 domain). In this study, we confirmed that AtHIR1 and AtHIR2 form complexes with RPS2 in Arabidopsis and Nicotiana benthamiana using a pulldown assay and fluorescence resonance energy transfer (FRET) analysis. Arabidopsis has four HIR family genes (AtHIR1-4). All AtHIR proteins could form homo- and hetero-oligomers in vivo and were enriched in membrane microdomains of the plasma membrane. The mRNA levels of all except AtHIR4 were significantly induced by microbe-associated molecular patterns, such as the bacterial flagellin fragment flg22. Athir2-1 and Athir3-1 mutants allowed more growth of Pto DC3000 AvrRpt2, but not Pto DC3000, indicating that these mutations reduce RPS2-mediated ETI but do not affect basal resistance to the virulent strain. Overexpression of AtHIR1 and AtHIR2 reduced growth of Pto DC3000. Taken together, the results show that the AtHIR proteins are physically associated with RPS2, are localized in membrane microdomains, and quantitatively contribute to RPS2-mediated ETI.
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