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

DongHyuk Lee, Neeraj K. Lal, Zuh-Jyh Daniel Lin, Shisong Ma, Jun Liu, Bardo Castro, Tania Toruño, Savithramma P. Dinesh-Kumar and Gitta Coaker ()
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DongHyuk Lee: University of California
Neeraj K. Lal: University of California
Zuh-Jyh Daniel Lin: University of California
Shisong Ma: University of California
Jun Liu: University of California
Bardo Castro: University of California
Tania Toruño: University of California
Savithramma P. Dinesh-Kumar: University of California
Gitta Coaker: University of California

Nature Communications, 2020, vol. 11, issue 1, 1-16

Abstract: 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.

Date: 2020
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DOI: 10.1038/s41467-020-15601-5

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