Release of a ubiquitin brake activates OsCERK1-triggered immunity in rice

• 成果类型: Article
• 署名作者: Wang, Gang; Chen, Xi; Yu, Chengzhi; Shi, Xiaobao; Lan, Wenxian; Gao, Chaofeng; Yang, Jun; Dai, Huiling; Zhang, Xiaowei; Zhang, Huili; Zhao, Boyu; Xie, Qi; Yu, Nan; He, Zuhua; Zhang, Yu; Wang, Ertao
• 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; Fujian Agriculture & Forestry University; Shanghai Normal University; Chinese Academy of Sciences; Institute of Genetics & Developmental Biology, CAS; ShanghaiTech University
• 刊物名称: Nature
• ISSN/ISSBN: 0028-4611
• DOI: 10.1038/s41586-024-07418-9
• 发表日期: 2024-05-30
• 页码: 1158-+
• 关键词: chitin perception; receptor kinase; innate immunity; cell-death; xplor-nih; ligase; DEFENSE; cerk1; peptidoglycan; mutagenesis

摘要

Plant pattern-recognition receptors perceive microorganism-associated molecular patterns to activate immune signalling(1,2). Activation of the pattern-recognition receptor kinase CERK1 is essential for immunity, but tight inhibition of receptor kinases in the absence of pathogen is crucial to prevent autoimmunity(3,4). Here we find that the U-box ubiquitin E3 ligase OsCIE1 acts as a molecular brake to inhibit OsCERK1 in rice. During homeostasis, OsCIE1 ubiquitinates OsCERK1, reducing its kinase activity. In the presence of the microorganism-associated molecular pattern chitin, active OsCERK1 phosphorylates OsCIE1 and blocks its E3 ligase activity, thus releasing the brake and promoting immunity. Phosphorylation of a serine within the U-box of OsCIE1 prevents its interaction with E2 ubiquitin-conjugating enzymes and serves as a phosphorylation switch. This phosphorylation site is conserved in E3 ligases from plants to animals. Our work identifies a ligand-released brake that enables dynamic immune regulation.