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FEBS Lett. 2016 May;590(10):1477-87. doi: 10.1002/1873-3468.12191. Epub 2016 May 17.

LYR3, a high-affinity LCO-binding protein of Medicago truncatula, interacts with LYK3, a key symbiotic receptor.

Author information

1
LIPM, Université de Toulouse, INRA, CNRS, Castanet-Tolosan, France.
2
Plateforme Imagerie-Microscopie, Fédération de Recherche FR3450 - Agrobiosciences, Interactions et Biodiversité, CNRS, Université de Toulouse, UPS, Castanet-Tolosan, France.
3
Fédération de Recherche FR3450 - Agrobiosciences, Interactions et Biodiversité, CNRS, Université de Toulouse, UPS, Castanet-Tolosan, France.
4
Institut de Pharmacologie et de Biologie Structurale, Université de Toulouse, CNRS, UPS, Toulouse, France.

Abstract

LYR3, LYK3, and NFP are lysin motif-containing receptor-like kinases (LysM-RLKs) from Medicago truncatula, involved in perception of symbiotic lipo-chitooligosaccharide (LCO) signals. Here, we show that LYR3, a high-affinity LCO-binding protein, physically interacts with LYK3, a key player regulating symbiotic interactions. In vitro, LYR3 is phosphorylated by the active kinase domain of LYK3. Fluorescence lifetime imaging/Förster resonance energy transfer (FLIM/FRET) experiments in tobacco protoplasts show that the interaction between LYR3 and LYK3 at the plasma membrane is disrupted or inhibited by addition of LCOs. Moreover, LYR3 attenuates the cell death response, provoked by coexpression of NFP and LYK3 in tobacco leaves.

KEYWORDS:

FLIM/FRET; LysM-RLK; Medicago truncatula; lipo-chitooligosaccharides; membrane receptor complex; phosphoproteomics

PMID:
27129432
DOI:
10.1002/1873-3468.12191
[Indexed for MEDLINE]
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