NADPH oxidase activity is required for ER stress survival in plants

Plant J. 2018 Dec;96(6):1106-1120. doi: 10.1111/tpj.14091. Epub 2018 Oct 23.

Abstract

In all eukaryotes, the unfolded protein response (UPR) relieves endoplasmic reticulum (ER) stress, which is a potentially lethal condition caused by the accumulation of misfolded proteins in the ER. In mammalian and yeast cells, reactive oxygen species (ROS) generated during ER stress attenuate the UPR, negatively impacting cell survival. In plants, the relationship between the UPR and ROS is less clear. Although ROS develop during ER stress, the sources of ROS linked to ER stress responses and the physiological impact of ROS generation on the survival from proteotoxic stress are yet unknown. Here we show that in Arabidopsis thaliana the respiratory burst oxidase homologs, RBOHD and RBOHF, contribute to the production of ROS during ER stress. We also demonstrate that during ER stress RBOHD and RBOHF are necessary to properly mount the adaptive UPR and overcome temporary and chronic ER stress situations. These results ascribe a cytoprotective role to RBOH-generated ROS in the defense from proteotoxic stress in an essential organelle, and support a plant-specific feature of the UPR management among eukaryotes.

Keywords: Arabidopsis thaliana; RBOHD; RBOHF; ER stress; Unfolded protein response; reactive oxygen species.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Arabidopsis / enzymology*
  • Arabidopsis / metabolism
  • Arabidopsis Proteins / metabolism*
  • Cell Death
  • Endoplasmic Reticulum Stress*
  • Hydrogen Peroxide / metabolism
  • NADPH Oxidases / metabolism*
  • Unfolded Protein Response

Substances

  • Arabidopsis Proteins
  • Hydrogen Peroxide
  • respiratory burst oxidase homolog D, Arabidopsis
  • NADPH Oxidases
  • RbohF protein, Arabidopsis