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Regulation of reactive oxygen species during plant immunity through phosphorylation and ubiquitination of RBOHD

Author

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  • DongHyuk Lee

    (University of California)

  • Neeraj K. Lal

    (University of California)

  • Zuh-Jyh Daniel Lin

    (University of California
    Donald Danforth Plant Science Center)

  • Shisong Ma

    (University of California
    University of Science and Technology of China)

  • Jun Liu

    (University of California
    Chinese Academy of Sciences)

  • Bardo Castro

    (University of California)

  • Tania Toruño

    (University of California)

  • Savithramma P. Dinesh-Kumar

    (University of California)

  • Gitta Coaker

    (University of California)

Abstract

Production of reactive oxygen species (ROS) is critical for successful activation of immune responses against pathogen infection. The plant NADPH oxidase RBOHD is a primary player in ROS production during innate immunity. However, how RBOHD is negatively regulated remains elusive. Here we show that RBOHD is regulated by C-terminal phosphorylation and ubiquitination. Genetic and biochemical analyses reveal that the PBL13 receptor-like cytoplasmic kinase phosphorylates RBOHD’s C-terminus and two phosphorylated residues (S862 and T912) affect RBOHD activity and stability, respectively. Using protein array technology, we identified an E3 ubiquitin ligase PIRE (PBL13 interacting RING domain E3 ligase) that interacts with both PBL13 and RBOHD. Mimicking phosphorylation of RBOHD (T912D) results in enhanced ubiquitination and decreased protein abundance. PIRE and PBL13 mutants display higher RBOHD protein accumulation, increased ROS production, and are more resistant to bacterial infection. Thus, our study reveals an intricate post-translational network that negatively regulates the abundance of a conserved NADPH oxidase.

Suggested Citation

  • DongHyuk Lee & Neeraj K. Lal & Zuh-Jyh Daniel Lin & Shisong Ma & Jun Liu & Bardo Castro & Tania Toruño & Savithramma P. Dinesh-Kumar & Gitta Coaker, 2020. "Regulation of reactive oxygen species during plant immunity through phosphorylation and ubiquitination of RBOHD," Nature Communications, Nature, vol. 11(1), pages 1-16, December.
    • Handle: RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-15601-5
    DOI: 10.1038/s41467-020-15601-5
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    Cited by:

    1. Jiaojiao Bai & Yuanyuan Zhou & Jianhang Sun & Kexin Chen & Yufang Han & Ranran Wang & Yanmin Zou & Mingshuo Du & Dongping Lu, 2023. "BIK1 protein homeostasis is maintained by the interplay of different ubiquitin ligases in immune signaling," Nature Communications, Nature, vol. 14(1), pages 1-14, December.
    2. Yuhang Duan & Zhaoyun Wang & Yuan Fang & Zhangxin Pei & Hong Hu & Qiutao Xu & Hao Liu & Xiaolin Chen & Chaoxi Luo & Junbin Huang & Lu Zheng & Xiaoyang Chen, 2024. "A secreted fungal laccase targets the receptor kinase OsSRF3 to inhibit OsBAK1–OsSRF3-mediated immunity in rice," Nature Communications, Nature, vol. 15(1), pages 1-19, December.

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