Diacylglycerol pyrophosphate binds and inhibits the glyceraldehyde-3-phosphate dehydrogenase in barley aleurone

Astorquiza, Paula Luján; Usorach, Javier; Racagni, G.; Villasuso, Ana Laura

doi:10.1016/j.plaphy.2016.01.012

Cited by 10 publications

(4 citation statements)

References 38 publications

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“…OsGAPDH has been reported to be a submergence-related gene in rice (Pillai, Lihuang, & Akiyama, 2002), while overexpression of GAPC alleviates salt toxicity by regulating hydrogen peroxide levels (Zhang et al, 2011). Another study showed that both the expression levels and enzyme activity of GAPC are increased when plants are treated with ABA (Astorquiza, Usorach, Racagni, & Villasuso, 2016). GAPC proteins are involved in seed ageing and programmed cell death (Gani et al, 2016).…”

Section: Introductionmentioning

confidence: 99%

Retracted: Cytosolic glyceraldehyde‐3‐phosphate dehydrogenase 2/5/6 increase drought tolerance via stomatal movement and reactive oxygen species scavenging in wheat

Zhang

Lei

Deng

et al. 2020

Plant Cell & Environment

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Drought is a major threat to wheat growth and crop productivity. However, there has been only limited success in developing drought‐hardy cultivars. This lack of progress is due, at least in part, to a lack of understanding of the molecular mechanisms of drought tolerance in wheat. Here, we evaluated the potential role of three cytosolic glyceraldehyde‐3‐phosphate dehydrogenases (TaGAPC2/5/6) under drought stress in wheat and Arabidopsis. We found that TaGAPC2/5/6 all positively responded to drought stress via reactive oxygen species (ROS) scavenging and stomatal movement. The results of yeast co‐transformation and electrophoretic mobility shift assay showed that TaWRKY33 acted as a direct regulator of TaGAPC2/5/6 genes. The dual luciferase reporter assay indicated that TaWRKY33 positively activated the expression of TaGAPC2/5/6. The results of bimolecular fluorescence complementation and yeast two‐hybrid system demonstrated that TaGAPC2/5/6 interacted with phospholipase Dδ (PLDδ). We then demonstrated that TaGAPC2/5/6 positively promoted the activity of TaPLDδ in vitro and in vivo. Furthermore, lower PLDδ activity in RNAi wheat could lead to less PA accumulation, causing higher stomatal aperture sizes under drought stress. In summary, our results establish a new positive regulatory mechanism of TaGAPCs which helps wheat fine‐tune their drought responses.

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Section: Introductionmentioning

confidence: 99%

Retracted: Cytosolic glyceraldehyde‐3‐phosphate dehydrogenase 2/5/6 increase drought tolerance via stomatal movement and reactive oxygen species scavenging in wheat

Zhang

Lei

Deng

et al. 2020

Plant Cell & Environment

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“…One important avenue for future research is to carefully investigate whether there are indeed specific DGPP binding proteins, and then to explore in detail the interaction of those proteins with both PA and DGPP. Only one published study has looked at DGPP binding proteins to date [ 31 ].…”

Section: Resultsmentioning

confidence: 99%

“…In the case of PA, the specific binding of proteins is likely driven by the unique physical chemical properties of this lipid, namely the ionization properties and spontaneous curvature. In the case of DGPP, only cytosolic GAPDH from Hordeum vulgare has been identified as a potential binding protein [ 31 ]. The Lys residues in the NAD+ binding site of GAPDH have been reported to be very active in numerous activities including the stable bonds formed with the phosphate group of phosphatidylserine (PS) [ 32 ], and may be responsible for the identification of GAPDH in the DGPP binding screen.…”

Section: Introductionmentioning

confidence: 99%

The Electrostatic Basis of Diacylglycerol Pyrophosphate—Protein Interaction

Graber

Kwarteng

Lange

et al. 2022

Cells

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Diacylglycerol pyrophosphate (DGPP) is an anionic phospholipid formed in plants, yeast, and parasites under multiple stress stimuli. It is synthesized by the phosphorylation action of phosphatidic acid (PA) kinase on phosphatidic acid, a signaling lipid with multifunctional properties. PA functions in the membrane through the interaction of its negatively charged phosphomonoester headgroup with positively charged proteins and ions. DGPP, like PA, can interact electrostatically via the electrostatic-hydrogen bond switch mechanism but differs from PA in its overall charge and shape. The formation of DGPP from PA alters the physicochemical properties as well as the structural dynamics of the membrane. This potentially impacts the molecular and ionic binding of cationic proteins and ions with the DGPP enriched membrane. However, the results of these important interactions in the stress response and in DGPP’s overall intracellular function is unknown. Here, using 31P MAS NMR, we analyze the effect of the interaction of low DGPP concentrations in model membranes with the peptides KALP23 and WALP23, which are flanked by positively charged Lysine and neutral Tryptophan residues, respectively. Our results show a significant effect of KALP23 on the charge of DGPP as compared to WALP23. There was, however, no significant effect on the charge of the phosphomonoester of DGPP due to the interaction with positively charged lipids, dioleoyl trimethylammonium propane (DOTAP) and dioleoyl ethyl-phosphatidylcholine (EtPC). Divalent calcium and magnesium cations induce deprotonation of the DGPP headgroup but showed no noticeable differences on DGPP’s charge. Our results lead to a novel model for DGPP—protein interaction.

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“…PA mediates cellular processes through several modes of action. These include binding to its targeted proteins to modulate their activity and modifying the biophysical properties of the membrane (Villasuso et al, 2014;Astorquiza et al, 2016;Pokotylo et al, 2018). PA acts as a signalling lipid in the plant's response to the cold.…”

Section: Introductionmentioning

confidence: 99%

Differential phosphatidic acid metabolism in barley leaves and roots induced by chilling temperature

Margutti

Gaveglio

Reyna

et al. 2018

Plant Physiology and Biochemistry

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Diacylglycerol pyrophosphate binds and inhibits the glyceraldehyde-3-phosphate dehydrogenase in barley aleurone

Cited by 10 publications

References 38 publications

Retracted: Cytosolic glyceraldehyde‐3‐phosphate dehydrogenase 2/5/6 increase drought tolerance via stomatal movement and reactive oxygen species scavenging in wheat

Retracted: Cytosolic glyceraldehyde‐3‐phosphate dehydrogenase 2/5/6 increase drought tolerance via stomatal movement and reactive oxygen species scavenging in wheat

The Electrostatic Basis of Diacylglycerol Pyrophosphate—Protein Interaction

Differential phosphatidic acid metabolism in barley leaves and roots induced by chilling temperature

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