Phosphorylation of plasma membrane H+-ATPase Thr881 participates in light-induced stomatal opening

Plasma membrane (PM) H + -ATPase is crucial for light-induced stomatal opening and phosphorylation of a penultimate residue, Thr948 (pen-Thr, numbering according to Arabidopsis AHA1) is required for enzyme activation. In this study, a comprehensive phosphoproteomic analysis using guard cell protoplasts from Vicia faba shows that both red and blue light increase the phosphorylation of Thr881, of PM H + -ATPase. Light-induced stomatal opening and the blue light-induced increase in stomatal conductance are reduced in transgenic Arabidopsis plants expressing mutant AHA1-T881A in aha1–9 , whereas the blue light-induced phosphorylation of pen-Thr is unaffected. Auxin and photosynthetically active radiation induce the phosphorylation of both Thr881 and pen-Thr in etiolated seedlings and leaves, respectively. The dephosphorylation of phosphorylated Thr881 and pen-Thr are mediated by type 2 C protein phosphatase clade D isoforms. Taken together, Thr881 phosphorylation, in addition of the pen-Thr phosphorylation, are important for PM H + -ATPase function during physiological responses, such as light-induced stomatal opening in Arabidopsis thaliana . Comprehensive phosphoproteomic analysis using guard cell protoplasts revealed that Thr881 phosphorylation in addition of a penultimate residue, Thr948 of plasma membrane H + -ATPase are important for its function and light-induced stomatal opening.