Статья

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

Donghyuk LeeDepartment of Plant Pathology, College of Agricultural and Environmental Sciences, University of California, Davis, CA, 95616, USANeeraj LalDepartment of Plant Biology and the Genome Center, College of Biological Sciences, University of California, Davis, CA, 95616, USAZuh-Jyh Daniel LinDepartment of Plant Pathology, College of Agricultural and Environmental Sciences, University of California, Davis, CA, 95616, USAShisong MaDepartment of Plant Biology and the Genome Center, College of Biological Sciences, University of California, Davis, CA, 95616, USAJun LiuDepartment of Plant Pathology, College of Agricultural and Environmental Sciences, University of California, Davis, CA, 95616, USABardo CastroDepartment of Plant Pathology, College of Agricultural and Environmental Sciences, University of California, Davis, CA, 95616, USATania Y. ToruñoDepartment of Plant Pathology, College of Agricultural and Environmental Sciences, University of California, Davis, CA, 95616, USASavithramma P. Dinesh‐KumarDepartment of Plant Biology and the Genome Center, College of Biological Sciences, University of California, Davis, CA, 95616, USAGitta CoakerDepartment of Plant Pathology, College of Agricultural and Environmental Sciences, University of California, Davis, CA, 95616, USA. [email protected]

2020en

ABI

Аннотация

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.

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Идентификаторы

DOI: 10.1038/s41467-020-15601-5

Цитирования и источники

Цитирований: 2Использованных источников: 0

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