Activation of a helper NLR by plant and bacterial TIR immune signaling

• 成果类型: Article
• 署名作者: Yu, Hua; Xu, Weiying; Chen, Sisi; Wu, Xiaoxian; Rao, Weiwei; Liu, Xiaoxiao; Xu, Xiaoyan; Chen, Jingqi; Nishimura, Marc T.; Zhang, Yu; Wan, Li
• 署名单位: Chinese Academy of Sciences; Center for Excellence in Molecular Plant Sciences, CAS; Chinese Academy of Sciences; University of Chinese Academy of Sciences, CAS; Colorado State University System; Colorado State University Fort Collins
• 刊物名称: SCIENCE
• ISSN/ISSBN: 0036-13602
• DOI: 10.1126/science.adr3150
• 发表日期: 2024-12-20
• 页码: 1413-1420
• 关键词: domains; resistosome; receptors; complex

摘要

Plant intracellular nucleotide-binding leucine-rich repeat (NLR) receptors with an N-terminal Toll/interleukin-1 receptor (TIR) domain sense pathogen effectors to initiate immune signaling. TIR domains across different kingdoms have NADase activities and can produce phosphoribosyl adenosine monophosphate/diphosphate (pRib-AMP/ADP) or cyclic ADPR (cADPR) isomers. The lipase-like proteins EDS1 and PAD4 transduce immune signals from sensor TIR-NLRs to a helper NLR called ADR1, which executes immune function. We report the structure and function of an Arabidopsis EDS1-PAD4-ADR1 (EPA) heterotrimer in complex with pRib-AMP/ADP activated by plant or bacterial TIR signaling. 2 ' cADPR can be hydrolyzed into pRib-AMP and thus activate EPA signaling. Bacterial TIR domains producing 2 ' cADPR also activate EPA function. Our findings suggest that 2 ' cADPR may be the storage form of the unstable signaling molecule pRib-AMP.