J Integr Plant Biol ›› 2024, Vol. 66 ›› Issue (7): 1459-1480.DOI: 10.1111/jipb.13666  cstr: 32098.14.jipb.13666

所属专题： Plant-biotic interaction； SDGs 目标2: 零饥饿； Rice

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  • 收稿日期:2023-10-29 接受日期:2024-03-21 出版日期:2024-07-01 发布日期:2024-07-12

OsATL32 ubiquitinates the reactive oxygen species-producing OsRac5–OsRbohB module to suppress rice immunity

Yuqing Yan1,2,3, Hui Wang1,2,3, Yan Bi1,2,3, Jiajing Wang1,2,3, Muhammad Noman1,2,3, Dayong Li1,2,3 and Fengming Song1,2,3*   

  1. 1. National Key Laboratory for Rice Biology and Breeding, Institute of Biotechnology, Zhejiang University, Hangzhou 310058, China
    2. Ministry of Agriculture Key Laboratory of Molecular Biology of Crop Pathogens and Insect Pests, Institute of Biotechnology, Zhejiang University, Hangzhou 310058, China
    3. Key Laboratory of Biology of Crop Pathogens and Insects of Zhejiang Province, Institute of Biotechnology, Zhejiang University, Hangzhou 310058, China
    *Correspondence: Fengming Song (fmsong@zju.edu.cn)
  • Received:2023-10-29 Accepted:2024-03-21 Online:2024-07-01 Published:2024-07-12

Abstract: Ubiquitination-mediated protein degradation is integral to plant immunity, with E3 ubiquitin ligases acting as key factors in this process. Here, we report the functions of OsATL32, a plasma membrane-localized Arabidopsis Tóxicos En Levadura (ATL)-type E3 ubiquitin ligase, in rice (Oryza sativa) immunity and its associated regulatory network. We found that the expression of OsATL32 is downregulated in both compatible and incompatible interactions between rice and the rice blast fungus Magnaporthe oryzae. The OsATL32 protein level declines in response to infection by a compatible M. oryzae strain or to chitin treatment. OsATL32 negatively regulates rice resistance to blast and bacterial leaf blight diseases, as well as chitin-triggered immunity. Biochemical and genetic studies revealed that OsATL32 suppresses pathogen-induced reactive oxygen species (ROS) accumulation by mediating ubiquitination and degradation of the ROS- producing OsRac5–OsRbohB module, which enhances rice immunity against M. oryzae. The protein phosphatase PHOSPHATASE AND TENSIN HOMOLOG enhances rice blast resistance by dephosphorylating OsATL32 and promoting its degradation, preventing its negative effect on rice immunity. This study provides insights into the molecular mechanism by which the E3 ligase OsATL32 targets a ROS-producing module to undermine rice immunity.

Key words: E3 ligase OsATL32, OsRac5–OsRbohB module, phosphatase OsPTEN, reactive oxygen species, rice immunity

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