Cytosolic Glyceraldehyde-3-Phosphate Dehydrogenases Interact with Phospholipase Dδ to Transduce Hydrogen Peroxide Signals in the Arabidopsis Response to Stress

Reactive oxygen species (ROS) are produced in plants under various stress conditions and serve as important mediators in plant responses to stresses. Here, we show that the cytosolic glycolytic enzymes glyceraldehyde-3-phosphate dehydrogenases (GAPCs) interact with the plasma membrane-associated phospholipase D (PLD delta) to transduce the ROS hydrogen peroxide (H2O2) signal in Arabidopsis thaliana. Genetic ablation of PLD delta impeded stomatal response to abscisic acid (ABA) and H2O2, placing PLD delta downstream of H2O2 in mediating ABA-induced stomatal closure. To determine the molecular link between H2O2 and PLD delta, GAPC1 and GAPC2 were identified to bind to PLD delta, and the interaction was demonstrated by coprecipitation using proteins expressed in Escherichia coli and yeast, surface plasmon resonance, and bimolecular fluorescence complementation. H2O2 promoted the GAPC-PLD delta interaction and PLD delta activity. Knockout of GAPCs decreased ABA- and H2O2-induced activation of PLD and stomatal sensitivity to ABA. The loss of GAPCs or PLD delta rendered plants less responsive to water deficits than the wild type. The results indicate that the H2O2-promoted interaction of GAPC and PLD delta may provide a direct connection between membrane lipid-based signaling, energy metabolism and growth control in the plant response to ROS and water stress.