An F‐box protein attenuates fungal xylanase‐triggered immunity by destabilizing LRR‐RLP NbEIX2 in a SOBIR1‐dependent manner

• DOI: 10.1111/nph.18509
• Publication Date: 2022-09-24T11:03:29Z
• Authors: Nan Wang; Zhiyuan Yin; Yaning Zhao; Jinghao Wang; Yong Pei; Peiyun Ji; Paul Daly; Zhengpeng Li; Daolong Dou; Lihui Wei
• Keywords: Nicotiana; Protein Domains; F-Box Proteins; Ubiquitin-Protein Ligases; Phosphotransferases; Signal Transduction

Receptor-like proteins (RLPs) lacking the cytoplasmic kinase domain play crucial roles in plant growth, development and immunity. However, what remains largely elusive is whether RLP protein levels are fine-tuned by E3 ubiquitin ligases, which employed receptor-like kinases for signaling attenuation. Nicotiana benthamiana NbEIX2 a leucine-rich repeat (LRR-RLP) that mediates fungal xylanase-triggered Here we show associates with an F-box NbPFB1, promotes degradation likely forming SCF ligase complex, negatively regulates NbEIX2-mediated immune responses. undergoes ubiquitination proteasomal planta. Interestingly, without its tail still associated destabilized NbPFB1. In addition, NbPFB1 also destabilizes NbSOBIR1, co-receptor of LRR-RLPs, fails to promote sobir1 mutant. Our findings reveal distinct model degradation, indirectly SOBIR1-dependent manner.