LORE receptor homomerization is required for 3‐hydroxydecanoic acid‐induced immune signaling and determines the natural variation of immunosensitivity within the Arabidopsis genus

Summary The S‐domain‐type receptor‐like kinase (SD‐RLK) LIPOOLIGOSACCHARIDE‐SPECIFIC REDUCED ELICITATION (LORE) from Arabidopsis thaliana is a pattern recognition receptor that senses medium‐chain 3‐hydroxy fatty acids, such as 3‐hydroxydecanoic acid (3‐OH‐C10:0), to activate pattern‐triggered immun...

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Bibliographic Details
Published in:	The New phytologist Vol. 242; no. 5; pp. 2163 - 2179
Main Authors:	Eschrig, Sabine, Schäffer, Milena, Shu, Lin‐Jie, Illig, Tina, Eibel, Sonja, Fernandez, Atiara, Ranf, Stefanie
Format:	Journal Article
Language:	English
Published:	England Wiley Subscription Services, Inc 01-06-2024
Subjects:	Amino acids Arabidopsis Chimeras Fatty acids Fluorescence G‐type lectin homomerization Intracellular signalling Kinases Lipooligosaccharides LORE Pattern recognition pattern recognition receptor Pattern recognition receptors pattern‐triggered immunity Reactive oxygen species Receptors receptor‐like kinase S‐domain Transmembrane domains G‐type lectin S‐domain LORE pattern‐triggered immunity receptor‐like kinase pattern recognition receptor homomerization
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Summary:	Summary The S‐domain‐type receptor‐like kinase (SD‐RLK) LIPOOLIGOSACCHARIDE‐SPECIFIC REDUCED ELICITATION (LORE) from Arabidopsis thaliana is a pattern recognition receptor that senses medium‐chain 3‐hydroxy fatty acids, such as 3‐hydroxydecanoic acid (3‐OH‐C10:0), to activate pattern‐triggered immunity. Here, we show that LORE homomerization is required to activate 3‐OH‐C10:0‐induced immune signaling. Fluorescence lifetime imaging in Nicotiana benthamiana demonstrates that AtLORE homomerizes via the extracellular and transmembrane domains. Co‐expression of AtLORE truncations lacking the intracellular domain exerts a dominant negative effect on AtLORE signaling in both N. benthamiana and A. thaliana, highlighting that homomerization is essential for signaling. Screening for 3‐OH‐C10:0‐induced reactive oxygen species production revealed natural variation within the Arabidopsis genus. Arabidopsis lyrata and Arabidopsis halleri do not respond to 3‐OH‐C10:0, although both possess a putative LORE ortholog. Both LORE orthologs have defective extracellular domains that bind 3‐OH‐C10:0 to a similar level as AtLORE, but lack the ability to homomerize. Thus, ligand binding is independent of LORE homomerization. Analysis of AtLORE and AlyrLORE chimera suggests that the loss of AlyrLORE homomerization is caused by several amino acid polymorphisms across the extracellular domain. Our findings shed light on the activation mechanism of LORE and the loss of 3‐OH‐C10:0 perception within the Arabidopsis genus.
Bibliography:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23
ISSN:	0028-646X 1469-8137
DOI:	10.1111/nph.19715