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Specific ER quality control components required for biogenesis of the plant innate immune receptor EFR
Open accessAbstract
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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“In summary, mutations of GII or UGGT genes impair glycoprotein folding and cause ER retention and/or degradation with loss of function [10,385].”
From GANAB and N-Glycans Substrates Are Relevant in Human Physiology, Polycystic Pathology and Multiple Sclerosis: A Review (2022) · cites this paper as [385]
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Metadata
- 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
- Publisher
- National Academy of Sciences
- Published
- 2009-09-15
- Volume
- 106
- Issue
- 37
- Pages
- 15973-15978
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC2747228
- 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
- green
- www.ncbi.nlm.nih.gov
- 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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