The Oleate-Stimulated Phospholipase D, PLDδ, and Phosphatidic Acid Decrease H2O2-Induced Cell Death in Arabidopsis

Hydrolysis of common membrane phospholipids occurs in response to various environmental stresses, but the control and cellular function of this hydrolysis are not fully understood. Hydrogen peroxide (H2O2) is a pivotal signaling molecule involved in various stress responses. Here, we show that the plasma membrane–bound phospholipase D, PLDδ, is activated in response to H2O2 and that the resulting phosphatidic acid (PA) functions to decrease H2O2-promoted programmed cell death. The Arabidopsis genome has 12 PLD genes, and knockout of PLDδ abolishes specifically the oleate-stimulated PLD activity. H2O2 treatment of Arabidopsis cells activates PLD enzyme activity, and ablation of PLDδ abolishes that activation. PLDδ-null cells display increased sensitivity to H2O2-induced cell death. The addition of PA to PLDδ-null cells mitigates the H2O2 effect, whereas suppression of the H2O2-induced PA formation in wild-type cells increases the effect. PLDδ-ablated plants exhibit increased susceptibility to stress. These results demonstrate that activation of oleate-stimulated PLDδ constitutes an important step in the plant response to H2O2 and increasing plant stress tolerance.