LYR3, a high‐affinity LCO‐binding protein of Medicago truncatula, interacts with LYK3, a key symbiotic receptor. Issue 10 (17th May 2016)

• Record Type: Journal Article
• Authors: Fliegmann, Judith; Jauneau, Alain; Pichereaux, Carole; Rosenberg, Charles; Gasciolli, Virginie; Timmers, Antonius C.J.; Burlet‐Schiltz, Odile; Cullimore, Julie; Bono, Jean‐Jacques
• Is Part Of: FEBS letters. Volume 590:Issue 10(2016)
• Page Start: 1477
• Page End: 1487
• Publication Date: 2016-05-17
• Subjects: FLIM/FRET -- lipo‐chitooligosaccharides -- LysM‐RLK -- Medicago truncatula -- membrane receptor complex -- phosphoproteomics; Biochemistry -- Periodicals; Biophysics -- Periodicals; Molecular biology -- Periodicals; Biochimie -- Périodiques; Biochemistry; Biophysics; Molecular biology; Periodicals; 572.05
• DOI: 10.1002/1873-3468.12191
• Languages: English
• ISSNs: 0014-5793

Abstract

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. Abstract : LYR3 interacts specifically with a key symbiotic receptor, LYK3. LYK3 phosphorylates LYR3 on five serine/threonine residues in vitro . The LYR3–LYK3 interaction is affected by the lipo‐chitooligosaccharide ligand of LYR3. LYR3 attenuates the cell death provoked by coexpression of LYK3 and NFP in tobacco.