Chen Jian, Zhang Xiaoxiao, Bernoux Maud, Rathjen John P, Dodds Peter N
Commonwealth Scientific and Industrial Research Organization, Agriculture and Food, Canberra, ACT 2601, Australia.
Research School of Biology, The Australian National University, Canberra, ACT 2600, Australia.
iScience. 2024 Jan 24;27(2):108817. doi: 10.1016/j.isci.2024.108817. eCollection 2024 Feb 16.
Plant Toll/interleukin-1 receptor/resistance protein (TIR) type nucleotide-binding and leucine-rich repeat immune receptors (NLRs) require enhanced disease susceptibility 1 (EDS1) family proteins and the helper NLRs NRG1 and ADR1 for immune activation. We show that the EDS1-SAG101b-NRG1 signaling pathway in is necessary for cell death signaling by TIR-NLRs from a range of plant species, suggesting a universal requirement for this module in TIR-NLR-mediated cell death in We also find that TIR domains physically associate with EDS1, PAD4, and SAG101 , independently of each other. Furthermore, NRG1 associates with SAG101b, but not with other EDS1 family members, via its C-terminal EP domain. Physical interaction between activated TIRs and EDS1 signaling complexes may facilitate the transfer of low abundance products of TIR catalytic activity or alter TIR catalytic activity to favor the production of EDS1 heterodimer ligands.
植物Toll/白细胞介素-1受体/抗性蛋白（TIR）型核苷酸结合和富含亮氨酸重复序列的免疫受体（NLR）需要增强的疾病易感性1（EDS1）家族蛋白以及辅助NLR蛋白NRG1和ADR1来激活免疫反应。我们发现，拟南芥中的EDS1-SAG101b-NRG1信号通路对于一系列植物物种的TIR-NLR介导的细胞死亡信号传导是必需的，这表明该模块在拟南芥的TIR-NLR介导的细胞死亡中具有普遍需求。我们还发现，TIR结构域彼此独立地与EDS1、PAD4和SAG101发生物理相互作用。此外，NRG1通过其C末端的EP结构域与SAG101b结合，但不与其他EDS1家族成员结合。活化的TIR与EDS1信号复合物之间的物理相互作用可能促进TIR催化活性的低丰度产物的转移，或改变TIR催化活性以利于EDS1异二聚体配体的产生。
