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

Author

Listed:
  • Gang Wang

    (Chinese Academy of Sciences
    The New Cornerstone Science Laboratory)

  • Xi Chen

    (Chinese Academy of Sciences
    The New Cornerstone Science Laboratory
    University of the Chinese Academy of Sciences)

  • Chengzhi Yu

    (Chinese Academy of Sciences
    University of the Chinese Academy of Sciences)

  • Xiaobao Shi

    (Chinese Academy of Sciences
    The New Cornerstone Science Laboratory
    University of the Chinese Academy of Sciences)

  • Wenxian Lan

    (Chinese Academy of Sciences)

  • Chaofeng Gao

    (Chinese Academy of Sciences
    The New Cornerstone Science Laboratory
    University of the Chinese Academy of Sciences)

  • Jun Yang

    (Chinese Academy of Sciences
    The New Cornerstone Science Laboratory)

  • Huiling Dai

    (Chinese Academy of Sciences
    The New Cornerstone Science Laboratory)

  • Xiaowei Zhang

    (Chinese Academy of Sciences
    The New Cornerstone Science Laboratory)

  • Huili Zhang

    (Fujian Agriculture and Forestry University)

  • Boyu Zhao

    (The New Cornerstone Science Laboratory
    Shanghai Normal University)

  • Qi Xie

    (Chinese Academy of Sciences)

  • Nan Yu

    (Shanghai Normal University)

  • Zuhua He

    (Chinese Academy of Sciences
    Shanghai Tech University)

  • Yu Zhang

    (Chinese Academy of Sciences)

  • Ertao Wang

    (Chinese Academy of Sciences
    The New Cornerstone Science Laboratory
    Shanghai Tech University)

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.

Suggested Citation

  • 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 & Ertao Wang, 2024. "Release of a ubiquitin brake activates OsCERK1-triggered immunity in rice," Nature, Nature, vol. 629(8014), pages 1158-1164, May.
    • Handle: RePEc:nat:nature:v:629:y:2024:i:8014:d:10.1038_s41586-024-07418-9
    DOI: 10.1038/s41586-024-07418-9
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