A method for functional testing constitutive and ligand-induced interactions of lysin motif receptor proteins.
Chimeric receptor
Lotus japonicus
LysM receptor-like kinase (LYK)
Lysin motif (LysM)
Receptor function
Journal
Plant methods
ISSN: 1746-4811
Titre abrégé: Plant Methods
Pays: England
ID NLM: 101245798
Informations de publication
Date de publication:
2020
2020
Historique:
received:
22
09
2019
accepted:
02
01
2020
entrez:
24
1
2020
pubmed:
24
1
2020
medline:
24
1
2020
Statut:
epublish
Résumé
Plant receptors with lysin motifs (LsyM) recognize microbial signals such as fungal chitin and lipo-chitooligosaccharidic Nod factors of nitrogen-fixing rhizobia. It is generally assumed that ligand-induced dimerization of LysM receptors is an essential step in activation of intracellular kinase domains and downstream signaling. Consequently, genes required for plant defense and establishment of symbiosis are expressed. We recently found that three LysM receptor proteins (namely LYK1, LYK4 and LYK5) of Interactions between ectodomains of LYK1, LYK4 and LYK5 were investigated by a chimeric receptor approach using hairy roots of the legume We present a method to functionally analyze constitutive and ligand-induced interactions of LysM-type proteins.
Sections du résumé
BACKGROUND
BACKGROUND
Plant receptors with lysin motifs (LsyM) recognize microbial signals such as fungal chitin and lipo-chitooligosaccharidic Nod factors of nitrogen-fixing rhizobia. It is generally assumed that ligand-induced dimerization of LysM receptors is an essential step in activation of intracellular kinase domains and downstream signaling. Consequently, genes required for plant defense and establishment of symbiosis are expressed. We recently found that three LysM receptor proteins (namely LYK1, LYK4 and LYK5) of
RESULTS
RESULTS
Interactions between ectodomains of LYK1, LYK4 and LYK5 were investigated by a chimeric receptor approach using hairy roots of the legume
CONCLUSION
CONCLUSIONS
We present a method to functionally analyze constitutive and ligand-induced interactions of LysM-type proteins.
Identifiants
pubmed: 31969929
doi: 10.1186/s13007-020-0551-4
pii: 551
pmc: PMC6964010
doi:
Types de publication
Journal Article
Langues
eng
Pagination
3Informations de copyright
© The Author(s) 2020.
Déclaration de conflit d'intérêts
Competing interestsThe authors declare that they have no competing interests.
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