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

© 2024 The Authors. New Phytologist © 2024 New Phytologist Foundation.

Détails bibliographiques
Publié dans:The New phytologist. - 1979. - 242(2024), 5 vom: 27. Juni, Seite 2163-2179
Auteur principal: Eschrig, Sabine (Auteur)
Autres auteurs: Schäffer, Milena, Shu, Lin-Jie, Illig, Tina, Eibel, Sonja, Fernandez, Atiara, Ranf, Stefanie
Format: Article en ligne
Langue:English
Publié: 2024
Accès à la collection:The New phytologist
Sujets:Journal Article Research Support, Non-U.S. Gov't G‐type lectin LORE S‐domain homomerization pattern recognition receptor pattern‐triggered immunity receptor‐like kinase
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520 |a 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 
650 4 |a Journal Article 
650 4 |a Research Support, Non-U.S. Gov't 
650 4 |a G‐type lectin 
650 4 |a LORE 
650 4 |a S‐domain 
650 4 |a homomerization 
650 4 |a pattern recognition receptor 
650 4 |a pattern‐triggered immunity 
650 4 |a receptor‐like kinase 
700 1 |a Schäffer, Milena  |e verfasserin  |4 aut 
700 1 |a Shu, Lin-Jie  |e verfasserin  |4 aut 
700 1 |a Illig, Tina  |e verfasserin  |4 aut 
700 1 |a Eibel, Sonja  |e verfasserin  |4 aut 
700 1 |a Fernandez, Atiara  |e verfasserin  |4 aut 
700 1 |a Ranf, Stefanie  |e verfasserin  |4 aut 
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773 1 8 |g volume:242  |g year:2024  |g number:5  |g day:27  |g month:06  |g pages:2163-2179 
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