Reactive Carbonyl Species Inhibit Blue-Light-Dependent Activation of the Plasma Membrane H+-ATPase and Stomatal Opening

Plant Cell Physiol. 2022 Aug 17;63(8):1168-1176. doi: 10.1093/pcp/pcac094.


Reactive oxygen species (ROS) play a central role in plant responses to biotic and abiotic stresses. ROS stimulate stomatal closure by inhibiting blue light (BL)-dependent stomatal opening under diverse stresses in the daytime. However, the stomatal opening inhibition mechanism by ROS remains unclear. In this study, we aimed to examine the impact of reactive carbonyl species (RCS), lipid peroxidation products generated by ROS, on BL signaling in guard cells. Application of RCS, such as acrolein and 4-hydroxy-(E)-2-nonenal (HNE), inhibited BL-dependent stomatal opening in the epidermis of Arabidopsis thaliana. Acrolein also inhibited H+ pumping and the plasma membrane H+-ATPase phosphorylation in response to BL. However, acrolein did not inhibit BL-dependent autophosphorylation of phototropins and the phosphorylation of BLUE LIGHT SIGNALING1 (BLUS1). Similarly, acrolein affected neither the kinase activity of BLUS1 nor the phosphatase activity of protein phosphatase 1, a positive regulator of BL signaling. However, acrolein inhibited fusicoccin-dependent phosphorylation of H+-ATPase and stomatal opening. Furthermore, carnosine, an RCS scavenger, partially alleviated the abscisic-acid- and hydrogen-peroxide-induced inhibition of BL-dependent stomatal opening. Altogether, these findings suggest that RCS inhibit BL signaling, especially H+-ATPase activation, and play a key role in the crosstalk between BL and ROS signaling pathways in guard cells.

Keywords: Blue light; H+-ATPase; Phototropin; RCS; ROS; Stomata.

MeSH terms

  • Acrolein / pharmacology
  • Arabidopsis Proteins* / metabolism
  • Arabidopsis* / metabolism
  • Cell Membrane / metabolism
  • Light
  • Plant Stomata / physiology
  • Proton-Translocating ATPases / metabolism
  • Reactive Oxygen Species / metabolism


  • Arabidopsis Proteins
  • Reactive Oxygen Species
  • Acrolein
  • Proton-Translocating ATPases