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

• Published in: The Plant cell Vol. 24; no. 5; pp. 2200 - 2212
• Main Authors: Guo, Liang, Devaiah, Shivakumar P., Narasimhan, Rama, Pan, Xiangqing, Zhang, Yanyan, Zhang, Wenhua, Wang, Xuemin
• Format: Journal Article
• Language: English
• Published: United States American Society of Plant Biologists 01.05.2012
• Subjects: Arabidopsis - drug effects; Arabidopsis - enzymology; Arabidopsis - genetics; Arabidopsis - metabolism; Cytosol - drug effects; Cytosol - enzymology; Cytosol - metabolism; Drought; Gene Expression Regulation, Plant - drug effects; Gene Expression Regulation, Plant - genetics; Glyceraldehyde-3-Phosphate Dehydrogenases - genetics; Glyceraldehyde-3-Phosphate Dehydrogenases - metabolism; Guard cells; Hydrogen Peroxide - pharmacology; Leaves; Phospholipase D - genetics; Phospholipase D - metabolism; Plant cells; Plant growth; Plant interaction; Plants; Plants, Genetically Modified - drug effects; Plants, Genetically Modified - enzymology; Plants, Genetically Modified - genetics; Plants, Genetically Modified - metabolism; Protein Binding; Proteins; Protoplasts; Reactive oxygen species
• ISSN: 1040-4651; 1532-298X
• DOI: 10.1105/tpc.111.094946

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 (PLDδ) to transduce the ROS hydrogen peroxide (H₂O₂) signal in Arabidopsis thaliana. Genetic ablation of PLDδ impeded stomatal response to abscisic acid (ABA) and H₂O₂, placing PLDδ downstream of H₂O₂ in mediating ABA-induced stomatal closure. To determine the molecular link between H₂O₂ and PLDδ, GAPC1 and GAPC2 were identified to bind to PLDδ, 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-PLDδ interaction and PLDδ activity. Knockout of GAPCs decreased ABA- and H₂O₂-induced activation of PLD and stomatal sensitivity to ABA. The loss of GAPCs or PLDδ rendered plants less responsive to water deficits than the wild type. The results indicate that the H₂O₂-promoted interaction of GAPC and PLDδ may provide a direct connection between membrane lipid–based signaling, energy metabolism and growth control in the plant response to ROS and water stress.