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Poster

Session: Session 1 Presenting Authors at Posters (Evens)

P-088 - Surface receptor-dependent NRG1 phosphorylation is important for TNL-mediated immunity

Tuesday, July 15, 2025
09:55 - 11:30  
Location: Confex Hall 3
Extracellular & Intracellular non-self recognition & signaling

    Presenting Author(s)

  • WH

    Wen R.H. Huang

    The Sainsbury Laboratory (TSL)
    Norwich, England, United Kingdom

    • Author(s)

  • RV

    Renzo Villena

    PhD Student
    The Sainsbury Laboratory
    Norwich, England, United Kingdom

  • HA

    Hee-Kyung Ahn

    Royal Society University Research Fellow
    University of Edinburgh
    EDINBURGH, Scotland, United Kingdom

  • SJ

    Sophie Louise Johnson

    The Sainsbury Laboratory (TSL)
    Norwich, England, United Kingdom

  • FM

    Frank L.H. Menke

    The Sainsbury Laboratory
    Norwich, England, United Kingdom

  • JJ

    Jonathan D. G. Jones

    Prof. Group leader
    The Sainsbury Laboratory
    Norwich, England, United Kingdom

Plants rely on a two-layered innate immune system to monitor the presence of immunogenic signals: cell-surface receptor-initiated pattern-triggered immunity (PTI) and intracellular nucleotide-binding leucine-rich repeat receptor (NLR)-initiated effector-triggered immunity (ETI). Interestingly, cell-surface receptors are required for full NLR-mediated plant immunity. NLRs are classified as sensor NLRs, which detect effectors, and helper NLRs, which mediate sensor NLR signalling. Sensor NLRs that carry a TIR domain at their N-termini require the helper NLRs ADR1 and NRG1 for full function. It has been reported that NRG1 oligomerises upon effector perception by TNLs. Our previous study demonstrated that EDS1 and SAG101 interact with the NRG1 oligomer in an EDS1-SAG101-NRG1 resistosome complex, which requires the co-activation of PTI and ETI. In this study, we show that NRG1 undergoes PTI-dependent phosphorylation, independent of effector recognition. Further investigations reveal that this phosphorylation is required for the formation of the EDS1-SAG101-NRG1 heterotrimer and resistosome, as well as TNL-mediated programmed cell death. These findings indicate that the EDS1-SAG101-NRG1 module acts as a checkpoint for PTI and ETI. However, alanine substitution of the identified phospho-sites in NRG1 significantly enhances host resistance against Pseudomonas syringae pv. tomato DC3000 in Nicotiana benthamiana. The molecular mechanisms underlying this observation will be reported.