Cited by 273Plant-Microbe Interactions and ImmunityEndoplasmic Reticulum Stress and DiseaseImmune Response and Inflammation

Specific ER quality control components required for biogenesis of the plant innate immune receptor EFR

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Li, Jing, Zhao-Hui, Chu, Batoux, Martine, Nekrasov, Vladimir, Roux, Milena, Chinchilla, Delphine, Zipfel, Cyril, Jones, Jonathan D. G.·2009·Proceedings of the National Academy of Sciences

Abstract

Plant innate immunity depends in part on recognition of pathogen-associated molecular patterns (PAMPs), such as bacterial flagellin, EF-Tu, and fungal chitin. Recognition is mediated by pattern-recognition receptors (PRRs) and results in PAMP-triggered immunity. EF-Tu and flagellin, and the derived peptides elf18 and flg22, are recognized in Arabidopsis by the leucine-rich repeat receptor kinases (LRR-RK), EFR and FLS2, respectively. To gain insights into the molecular mechanisms underlying PTI, we investigated EFR-mediated PTI using genetics. A forward-genetic screen for Arabidopsis elf18-insensitive (elfin) mutants revealed multiple alleles of calreticulin3 (CRT3), UDP-glucose glycoprotein glucosyl transferase (UGGT), and an HDEL receptor family member (ERD2b), potentially involved in endoplasmic reticulum quality control (ER-QC). Strikingly, FLS2-mediated responses were not impaired in crt3, uggt, and erd2b null mutants, revealing that the identified mutations are specific to EFR. A crt3 null mutant did not accumulate EFR protein, suggesting that EFR is a substrate for CRT3. Interestingly, Erd2b did not accumulate CRT3 protein, although they accumulate wild-type levels of other ER proteins. ERD2B seems therefore to be a specific HDEL receptor for CRT3 that allows its retro-translocation from the Golgi to the ER. These data reveal a previously unsuspected role of a specific subset of ER-QC machinery components for PRR accumulation in plant innate immunity.

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Crossref · 10.1073/pnas.0905532106

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Authors
Li, J., Zhao-Hui, C., Batoux, M., Nekrasov, V., Roux, M., Chinchilla, D., Zipfel, C., & Jones, J. D. G.
Affiliations
  • Norwich Research Park (GB)
  • University of Basel (CH)
Venue
Proceedings of the National Academy of Sciences
Published
2009-09-15
Volume
106
Issue
37
Pages
15973-15978
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W2129355294
Cited by
273
References
58
Citations by year
2026: 4 · 2025: 6 · 2024: 8 · 2023: 8 · 2022: 19 · 2021: 20 · 2020: 14 · 2019: 16 · 2018: 15 · 2017: 12 · 2016: 17 · 2015: 18 · 2014: 22 · 2013: 17 · 2012: 27
FWCI
31.00
Type
journal article
Language
en
Open access
Locations
  • Proceedings of the National Academy of Sciences (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
  • Zurich Open Repository and Archive (University of Zurich) (acceptedVersion)
  • UEA Digital Repository (University of East Anglia) (submittedVersion)
  • Zurich Open Repository and Archive (University of Zurich) (submittedVersion)
  • Zurich Open Repository and Archive (University of Zurich)
Funders
Biotechnology and Biological Sciences Research Council (BB/F021046/1, BB/E024874/1)
Topics
  • Life Sciences › Agricultural and Biological Sciences › Plant Science › Plant-Microbe Interactions and Immunity
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Endoplasmic Reticulum Stress and Disease
  • Life Sciences › Immunology and Microbiology › Immunology › Immune Response and Inflammation
Keywords
endoplasmic reticulum quality control, plant innate immunity, pattern-triggered immunity, protein accumulation, leucine-rich repeat receptor-like kinases, Arabidopsis thaliana, elf18, flg22, FLS2
MeSH terms
Alleles, Base Sequence, Endoplasmic Reticulum, Glucosyltransferases, Immunity, Innate, Membrane Proteins, Mutation, Plant Diseases, Protein Kinases, Signal Transduction, Genes, Plant, Arabidopsis, DNA Primers, Arabidopsis Proteins, Plants, Genetically Modified, Calreticulin, Pseudomonas syringae, Host-Pathogen Interactions

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