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Poster

Session: Session 1 Presenting Authors at Posters (Evens)

P-228 - A cell wall-associated kinase phosphorylates NLR immune receptor to negatively regulate resistosome formation

Tuesday, July 15, 2025
09:55 - 11:30  
Location: Confex Hall 3
Plant-virus Interactions (incl. Viromes, Evolution & Vectors)

    Author(s)

  • CZ

    Chenchen Zhong

    China Agricultural University
    Beijing, Beijing, China (People's Republic)

  • WL

    Wenli Li

    China Agricultural University
    Beijing, Beijing, China (People's Republic)

  • ZL

    Zhiyong Liu

    Professor
    Institute of Genetics and Developmental Biology, The Innovative Academy of Seed Design, Chinese Academy of Science
    Beijing, Beijing, China (People's Republic)

  • DL

    Dawei Li

    China Agricultural University
    Beijing, Beijing, China (People's Republic)

  • SD

    Savithramma P. Dinesh-Kumar

    College of Biological Sciences, University of California, Davis
    Davis, California, United States

    • Presenting Author(s)

  • YZ

    Yongliang Zhang (he/him/his)

    China Agricultural University
    Beijing, Beijing, China


Plants deploy intracellular NLRs to detect pathogen effectors and initiate immune responses. Although the activation mechanism of some plant NLRs forming resistosomes has been elucidated, whether NLR resistosome assembly is regulated to fine-tune immunity remains enigmatic. Here, we used an antiviral CNL, BSR1, as a model and demonstrate that BSR1 is phosphorylated. Using a proximity labeling approach, we identified a wall-associated kinase-like protein 20 (WAKL20) which negatively regulates BSR1-mediated immune responses by directly phosphorylating the Ser470 residue in the NB-ARC domain of BSR1. Mechanistically, Ser470 phosphorylation results in a steric clash of intramolecular domains of BSR1, thereby compromising BSR1 oligomerization. The phosphorylation site is conserved among multiple plant NLRs and our results show that WAKL20 participates in other NLRs-mediated immune response besides BSR1. Together, our data reveal phosphorylation as a mechanism for modulating plant resistosome assembly, and provide new insight into NLR-mediated plant immunity.