Release of a ubiquitin brake activates OsCERK1-triggered immunity in rice
Gang Wang,
Xi Chen,
Chengzhi Yu,
Xiaobao Shi,
Wenxian Lan,
Chaofeng Gao,
Jun Yang,
Huiling Dai,
Xiaowei Zhang,
Huili Zhang,
Boyu Zhao,
Qi Xie,
Nan Yu,
Zuhua He (),
Yu Zhang () and
Ertao Wang ()
Additional contact information
Gang Wang: Chinese Academy of Sciences
Xi Chen: Chinese Academy of Sciences
Chengzhi Yu: Chinese Academy of Sciences
Xiaobao Shi: Chinese Academy of Sciences
Wenxian Lan: Chinese Academy of Sciences
Chaofeng Gao: Chinese Academy of Sciences
Jun Yang: Chinese Academy of Sciences
Huiling Dai: Chinese Academy of Sciences
Xiaowei Zhang: Chinese Academy of Sciences
Huili Zhang: Fujian Agriculture and Forestry University
Boyu Zhao: The New Cornerstone Science Laboratory
Qi Xie: Chinese Academy of Sciences
Nan Yu: Shanghai Normal University
Zuhua He: Chinese Academy of Sciences
Yu Zhang: Chinese Academy of Sciences
Ertao Wang: Chinese Academy of Sciences
Nature, 2024, vol. 629, issue 8014, 1158-1164
Abstract:
Abstract Plant pattern-recognition receptors perceive microorganism-associated molecular patterns to activate immune signalling1,2. 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 autoimmunity3,4. 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.
Date: 2024
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DOI: 10.1038/s41586-024-07418-9
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