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Phosphatidic acid (PA) is involved in biotic and abiotic stress responses in plants. Here, we summarize quantitative lipidomics and real-time imaging used in PA studies and highlight recent studies of diacylglycerol (DAG) kinase (DGK) 5, an enzyme involved in PA biosynthesis, facilitating fine-tuning PA production for optimal stress responses in plants., Competing Interests: Declaration of interests There are no interests to declare., (Copyright © 2024 Elsevier Ltd. All rights reserved.)

Membrane lipidomes are dynamic and their changes generate lipid mediators affecting various biological processes. Phosphatidic acid (PA) has emerged as an important class of lipid mediators involved in a wide range of cellular and physiological responses in plants, animals, and microbes. The regulatory functions of PA have been studied primarily outside the nuclei, but an increasing number of recent studies indicates that some of the PA effects result from its action in nuclei. PA levels in nuclei are dynamic in response to stimuli. Changes in nuclear PA levels can result from activities of enzymes associated with nuclei and/or from movements of PA generated extranuclearly. PA has also been found to interact with proteins involved in nuclear functions, such as transcription factors and proteins undergoing nuclear translocation in response to stimuli. The nuclear action of PA affects various aspects of plant growth, development, and response to stress and environmental changes., Competing Interests: Declaration of Competing Interest The authors declare no conflict of interest., (Copyright © 2023 Elsevier Ltd. All rights reserved.)

Membrane fluidity, permeability, and surface charges are controlled by phospholipid metabolism and transport. Despite the importance of phosphatidic acid (PA) as a bioactive molecule, the mechanical properties of PA translocation and subcellular accumulation are unknown. Here, we used a mobilizable, highly responsive genetically encoded fluorescent indicator, green fluorescent protein (GFP)-N160 RbohD , to monitor PA dynamics in living cells. The majority of GFP-N160 RbohD accumulated at the plasma membrane and sensitively responded to changes in PA levels. Cellular, pharmacological, and genetic analyses illustrated that both salinity and abscisic acid rapidly enhanced GFP-N160 RbohD fluorescence at the plasma membrane, which mainly depended on hydrolysis of phospholipase D. By contrast, heat stress induced nuclear translocation of PA indicated by GFP-N160 RbohD through a process that required diacylglycerol kinase activity, as well as secretory and endocytic trafficking. Strikingly, we showed that gravity triggers asymmetric PA distribution at the root apex, a response that is suppressed by PLDζ2 knockout. The broad utility of the PA sensor will expand our mechanistic understanding of numerous lipid-associated physiological and cell biological processes and facilitate screening for protein candidates that affect the synthesis, transport, and metabolism of PA., (Copyright © 2022 The Authors. Published by Elsevier Inc. All rights reserved.)

Symbiotic rhizobium-legume interactions, such as root hair curling, rhizobial invasion, infection thread expansion, cell division and proliferation of nitrogen-fixing bacteroids, and nodule formation, involve extensive membrane synthesis, lipid remodeling and cytoskeleton dynamics. However, little is known about these membrane-cytoskeleton interfaces and related genes. Here, we report the roles of a major root phospholipase D (PLD), PLDα1, and its enzymatic product, phosphatidic acid (PA), in rhizobium-root interaction and nodulation. PLDα1 was activated and the PA content transiently increased in roots after rhizobial infection. Levels of PLDα1 transcript and PA, as well as actin and tubulin cytoskeleton-related gene expression, changed markedly during root-rhizobium interactions and nodule development. Pre-treatment of the roots of soybean seedlings with n-butanol suppressed the generation of PLD-derived PA, the expression of early nodulation genes and nodule numbers. Overexpression or knockdown of GmPLDα1 resulted in changes in PA levels, glycerolipid profiles, nodule numbers, actin cytoskeleton dynamics, early nodulation gene expression and hormone levels upon rhizobial infection compared with GUS roots. The transcript levels of cytoskeleton-related genes, such as GmACTIN, GmTUBULIN, actin capping protein 1 (GmCP1) and microtubule-associating protein (GmMAP1), were modified in GmPLDα1-altered hairy roots compared with those of GUS roots. Phosphatidic acid physically bound to GmCP1 and GmMAP1, which could be related to cytoskeletal changes in rhizobium-infected GmPLDα1 mutant roots. These data suggest that PLDα1 and PA play important roles in soybean-rhizobium interaction and nodulation. The possible underlying mechanisms, including PLDα1- and PA-mediated lipid signaling, membrane remodeling, cytoskeleton dynamics and related hormone signaling, are discussed herein., (© 2020 Society for Experimental Biology and John Wiley & Sons Ltd.)

Lipids function not only as the major structural components of cell membranes, but also as molecular messengers that transduce signals to trigger downstream signaling events in the cell. Phosphatidic acid (PA), the simplest and a minor class of glycerophospholipids, is a key intermediate for the synthesis of membrane and storage lipids, and also plays important roles in mediating diverse cellular and physiological processes in eukaryotes ranging from microbes to mammals and higher plants. PA comprises different molecular species that can act differently, and is found in virtually all organisms, tissues, and organellar membranes, with variations in total content and molecular species composition. The cellular levels of PA are highly dynamic in response to stimuli and multiple enzymatic reactions can mediate its production and degradation. Moreover, its unique physicochemical properties compared with other glycerophospholipids allow PA to influence membrane structure and dynamics, and interact with various proteins. PA has emerged as a class of new lipid mediators modulating various signaling and cellular processes via its versatile effects, such as membrane tethering, conformational changes, and enzymatic activities of target proteins, and vesicular trafficking., (© 2020 The Author(s). Published by Portland Press Limited on behalf of the Biochemical Society.)

The signalling lipid phosphatidic acid (PA) is involved in regulating various fundamental biological processes in plants. However, the mechanisms of PA action remain poorly understood because currently available methods for monitoring PA fail to determine the precise spatio-temporal dynamics of this messenger in living cells and tissues of plants. Here, we have developed PAleon, a PA-specific optogenetic biosensor that reports the concentration and dynamics of bioactive PA at the plasma membrane based on Förster resonance energy transfer (FRET). PAleon was sensitive enough to monitor physiological concentrations of PA in living cells and to visualize PA dynamics at subcellular resolution in tissues when they were challenged with abscisic acid (ABA) and salt stress. PAleon bioimaging revealed kinetics and tissue specificity of salt stress-triggered PA accumulation. Compared with wild-type Arabidopsis, the pldα1 mutant lacking phospholipase Dα1 (PLDα1) for PA generation showed delayed and reduced PA accumulation. Comparative analysis of wild type and pldα1 mutant indicated that cellular pH-modulated PA interaction with target proteins and PLD/PA-mediated salt tolerance. Application of the PA biosensor PAleon uncovered specific spatio-temporal PA dynamics in plant tissues. Our findings suggest that PA signalling integrates with cellular pH dynamics to mediate plant response to salt stress.

Phospholipase D (PLD) hydrolyzes membrane phospholipids to generate phosphatidic acid (PA). Both PLD and its lipid product PA are involved in various physiological processes, including plant response to pathogens. The PLD family is comprised of multiple members in higher plants, and PLDs have been reported to play positive and/or negative roles in plant immunity, depending on the types of pathogens and specific PLDs involved. Individual PLDs have distinguishable biochemical properties, such as Ca 2+ and phosphatidylinositide requirements. In addition, PLDs and PA are found to interact with various proteins in hormone and stress signaling. The different biochemical and regulatory properties of PLDs and PA shed light on the mechanisms for the functional diversity of PLDs in plant defense signaling and response., (Copyright © 2018 Elsevier B.V. All rights reserved.)

Circadian clocks play important roles in regulating cellular metabolism, but the reciprocal effect that metabolism has on the clock is largely unknown in plants. Here, we show that the central glycerolipid metabolite and lipid mediator phosphatidic acid (PA) interacts with and modulates the function of the core clock regulators LATE ELONGATED HYPOCOTYL (LHY) and CIRCADIAN CLOCK ASSOCIATED1 (CCA1) in Arabidopsis ( Arabidopsis thaliana ). PA reduced the ability of LHY and CCA1 to bind the promoter of their target gene TIMING OF CAB EXPRESSION1 Increased PA accumulation and inhibition of PA-producing enzymes had opposite effects on circadian clock outputs. Diurnal change in levels of several membrane phospholipid species, including PA, observed in wild type was lost in the LHY and CCA1 double knockout mutant. Storage lipid accumulation was also affected in the clock mutants. These results indicate that the interaction of PA with the clock regulator may function as a cellular conduit to integrate the circadian clock with lipid metabolism., (© 2019 American Society of Plant Biologists. All rights reserved.)

Transport of proteins containing a nuclear localization signal (NLS) into the nucleus is mediated by nuclear transport receptors called importins, typically dimmers of a cargo-binding α-subunit and a β-subunit that mediates translocation through the nuclear pore complexes (NPCs). However, how proteins without canonical NLS move into the nucleus is not well understood. Recent results indicate that phospholipids, such as phosphatidic acid, play important roles in the intracellular translocation of proteins between the nucleus and cytoplasm.

Phosphatidic acid (PA) has emerged as a class of cellular mediators involved in various cellular and physiological processes, but little is known about its mechanism of action. Here we show that PA interacts with werewolf (WER), a R2R3 MYB transcription factor involved in root hair formation. The PA-interacting region is confined to the end of the R2 subdomain. The ablation of the PA binding motif has no effect on WER binding to DNA, but abolishes its nuclear localization and its function in regulating epidermal cell fate. Inhibition of PA production by phospholipase Dζ also suppresses WER's nuclear localization, root hair formation, and elongation. These results suggest a role for PA in promoting protein nuclear localization.

Phosphatidic acid (PA) is a class of lipid messengers involved in a variety of physiological processes. To understand how PA mediates cell functions in plants, we used a PA affinity membrane assay to isolate PA-binding proteins from Camelina sativa followed by mass spectrometric sequencing. A cytosolic glyceraldehyde-3-phosphate dehydrogenase (GAPC) was identified to bind to PA, and detailed analysis was carried out subsequently using GAPC1 and GAPC1 from Arabidopsis. The PA and GAPC binding was abolished by the cation zinc whereas oxidation of GAPCs promoted the PA binding. PA had little impact on the GAPC catalytic activity in vitro, but the PA treatment of Arabidopsis seedlings induced proteolytic cleavage of GAPC2 and inhibited Arabidopsis seedling growth. The extent of PA inhibition was greater in GAPC-overexpressing than wild-type seedlings, but the greater PA inhibition was abolished by application of zinc to the seedling. The PA treatment also reduced the expression of genes involved in PA synthesis and utilization, and the PA-reduced gene expression was partially recovered by zinc treatment. These data suggest that PA binds to oxidized GAPDH and promotes its cleavage and that the PA and GAPC interaction may provide a signaling link coordinating carbohydrate and lipid metabolism.

Phosphatidic acid (PA) is recognized as an important class of lipid messengers. The cellular PA levels are dynamic; PA is produced and metabolized by several enzymatic reactions, including different phospholipases, lipid kinases, and phosphatases. PA interacts with various proteins and the interactions may modulate enzyme catalytic activities and/or tether proteins to membranes. The PA-protein interactions are impacted by changes in cellular pH and other effectors, such as cations. PA is involved in a wide range of cellular processes, including vesicular trafficking, cytoskeletal organization, secretion, cell proliferation, and survival. Manipulations of different PA production reactions alter cellular and organismal response to a wide range of abiotic and biotic stresses. Further investigations of PA's function and mechanisms of action will advance not only the understanding of cell signaling networks but also may lead to biotechnological and pharmacological applications.

Phosphatidic acid (PA) and phytosphingosine-1-phosphate (phyto-S1P) have both been identified as lipid messengers mediating plant response to abscisic acid (ABA). To determine the relationship of these messengers, we investigated the direct interaction of PA with Arabidopsis sphingosine kinases (SPHKs) that phosphorylate phytosphingosine to generate phyto-S1P. Two unique SPHK cDNAs were cloned from the annotated At4g21540 locus of Arabidopsis, and the two transcripts are differentially expressed in Arabidopsis tissues. Both SPHKs are catalytically active, phosphorylating various long-chain sphingoid bases (LCBs) and are associated with the tonoplast. They both interact with PA as demonstrated by lipid-filter binding, liposome binding, and surface plasmon resonance (SPR). SPHK1 and SPHK2 exhibited strong binding to 18:1/18:1, 16:0/18:1, and 16:0/18:2 PA, but poor binding to 16:0/16:0, 8:0/8:0, 18:0/18:0, and 18:2/18:2 PA. Surface dilution kinetics analysis indicates that PA stimulates SPHK activity by increasing the specificity constant through decreasing K(m)(B). The results show that the annotated At4g21540 locus is actually comprised of two separate SPHK genes. PA binds to both SPHKs, and the interaction promotes lipid substrate binding to the catalytic site of the enzyme. The PA-SPHK interaction depends on the PA molecular species. The data suggest that these two Arabidopsis SPHKs are molecular targets of PA, and the PA stimulation of SPHK is part of the signaling networks in Arabidopsis.

The activity of phospholipase D (PLD) in plants increases under different hyperosmotic stresses, such as dehydration, drought, and salinity. Recent results begin to shed light onto the involvement of PLD in response to water deficits and salinity. Different PLDs have unique and overlapping functions in these responses. PLDalpha1 promotes stomatal closure and reduces water loss. PLDalpha1 and PLDdelta are involved in seedling tolerance to salt stress. PLDalpha3 and PLDepsilon enhance plant growth and hyperosmotic tolerance. The different PLDs regulate the production of phosphatidic acid (PA) that is a key class of lipid mediators in plant response to environmental stresses. Further studies on the upstream regulators that activate different PLDs and the downstream effectors of PLDs and PA have the potential to unveil the linkage between the stimulus perception at the cell membrane to intracellular responses to drought and salinity stresses.

The phospholipase D (PLD) family in higher plants is composed of multiple members, and each of the Arabidopsis PLDs characterized displays distinguishable properties in activity regulation and/or lipid preferences. The molecular and biochemical heterogeneities of the plant PLDs play important roles in the timing, location, and amount of phosphatidic acid (PA) produced. PLD-catalyzed production of PA has been shown to play important roles in plant growth, development, and response to various stresses, including drought, salinity, freezing, and nutrient deficiency. PLD and PA affect cellular processes through different modes of action, including direct target protein binding and biophysical effects on cell membranes. Improved knowledge on the mechanism by which specific PLDs and PA mediate given plant responses will facilitate the understanding of the molecular processes that connect the stimulus perception on membranes to intracellular actions and physiological responses.

We determined the role of Phospholipase Dalpha1 (PLDalpha1) and its lipid product phosphatidic acid (PA) in abscisic acid (ABA)-induced production of reactive oxygen species (ROS) in Arabidopsis thaliana guard cells. The pldalpha1 mutant failed to produce ROS in guard cells in response to ABA. ABA stimulated NADPH oxidase activity in wild-type guard cells but not in pldalpha1 cells, whereas PA stimulated NADPH oxidase activity in both genotypes. PA bound to recombinant Arabidopsis NADPH oxidase RbohD (respiratory burst oxidase homolog D) and RbohF. The PA binding motifs were identified, and mutation of the Arg residues 149, 150, 156, and 157 in RbohD resulted in the loss of PA binding and the loss of PA activation of RbohD. The rbohD mutant expressing non-PA-binding RbohD was compromised in ABA-mediated ROS production and stomatal closure. Furthermore, ABA-induced production of nitric oxide (NO) was impaired in pldalpha1 guard cells. Disruption of PA binding to ABI1 protein phosphatase 2C did not affect ABA-induced production of ROS or NO, but the PA-ABI1 interaction was required for stomatal closure induced by ABA, H(2)O(2), or NO. Thus, PA is as a central lipid signaling molecule that links different components in the ABA signaling network in guard cells.

Activation of phospholipase D (PLD) produces phosphatidic acid (PA), a lipid messenger implicated in cell growth and proliferation, but direct evidence for PLD and PA promotion of growth at the organism level is lacking. Here we characterize a new PLD gene, PLD epsilon, and show that it plays a role in promoting Arabidopsis growth. PLD epsilon is mainly associated with the plasma membrane, and is the most permissive of all PLDs tested with respect to its activity requirements. Knockout (KO) of PLD epsilon decreases root growth and biomass accumulation, whereas over-expression (OE) of PLD epsilon enhances root growth and biomass accumulation. The level of PA was higher in OE plants, but lower in KO plants than in wild-type plants, and suppression of PLD-mediated PA formation by alcohol alleviated the growth-promoting effect of PLD epsilon. OE and KO of PLD epsilon had opposite effects on lateral root elongation in response to nitrogen. Increased expression of PLD epsilon also promoted root hair elongation and primary root growth under severe nitrogen deprivation. The results suggest that PLD epsilon and PA promote organism growth and play a role in nitrogen signaling. The lipid-signaling process may play a role in connecting membrane sensing of nutrient status to increased plant growth and biomass production.

Phosphatidic acid (PA) has emerged as a new class of lipid mediators involved in diverse cellular functions in plants, animals, and microorganisms. Considerable progress has been made recently on the production, cellular function, and mode of action of PA in the cell. The cellular levels of PA undergo dynamic changes in response to developmental and environmental stimuli. The production of signaling PA is mediated by families of multiple enzymes that regulate the timing, location, amount, and molecular species of PA. A number of PA target proteins have been identified, which include proteins involved in phosphorylation and dephosphorylation of proteins and lipids, as well as in G protein regulation, vesicular trafficking, and metabolism. PA mediates cellular functions through different modes of action, such as membrane tethering, modulation of enzymatic activities, and/or structural effects on cell membranes. The regulatory processes in which PA has been implicated include signaling pathways in cell growth, proliferation, reproduction, and responses to hormones and biotic and abiotic stresses.

Phospholipase D (PLD) and protein phosphatase 2C (PP2C) both play a role in mediating plant responses to abscisic acid (ABA). In this article, we show that PLD alpha 1 and its product, phosphatidic acid (PA), regulate a PP2C, ABI1, which is a negative regulator of ABA responses in Arabidopsis. Leaves from a T-DNA insertional mutant of PLD alpha 1 and PLD alpha 1-antisense plants lose more water than do wild-type plants. The stomatal closure of PLD alpha 1-null leaves is insensitive to ABA but is promoted by PA. ABA treatment promotes an increase in PA from phosphatidylcholine in wild type but not in PLD alpha 1-null cells. PLD alpha 1-derived PA binds to ABI1; the PA-ABI1 binding is demonstrated by coprecipitating PA with ABI1 from plant cells, measuring binding of PA from vesicles to ABI1, and assaying ABI1 bound to PA immobilized on a filter. Deletion and site-specific mutational analyses show that arginine 73 in ABI1 is essential for PA-ABI1 binding. PA binding decreases the phosphatase activity of ABI1. The lack of ABA-induced production of PA in PLD alpha 1-null cells results in a decrease in the association of ABI1 with the plasma membrane in response to ABA. These results indicate that PA produced by PLD alpha 1 inhibits the function of the negative regulator ABI1, thus promoting ABA signaling. The identification of ABI1 as a direct target of the lipid messenger PA provides a functional link between the two families of important signaling enzymes, PLD and PP2C.

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, PLDdelta, 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 PLDdelta abolishes specifically the oleate-stimulated PLD activity. H2O2 treatment of Arabidopsis cells activates PLD enzyme activity, and ablation of PLDdelta abolishes that activation. PLDdelta-null cells display increased sensitivity to H2O2-induced cell death. The addition of PA to PLDdelta-null cells mitigates the H2O2 effect, whereas suppression of the H2O2-induced PA formation in wild-type cells increases the effect. PLDdelta-ablated plants exhibit increased susceptibility to stress. These results demonstrate that activation of oleate-stimulated PLDdelta constitutes an important step in the plant response to H2O2 and increasing plant stress tolerance.

SUMMARY: Cytosolic glyceraldehyde‐3‐phosphate dehydrogenase (GAPC) is a glycolytic enzyme, but undergoes stress‐induced nuclear translocation for moonlighting. We previously reported that in response to heat stress, GAPC accumulated in the nucleus to modulate transcription and thermotolerance. Here we show a cellular and molecular mechanism that mediates heat‐induced nuclear translocation of cytosolic GAPC in Arabidopsis thaliana. Heat‐induced GAPC nuclear accumulation and plant heat tolerance were reduced in Arabidopsis phospholipase D (PLD) knockout mutants of pldδ and pldα1pldδ, but not of pldα1. These changes were restored to wild type by genetic complementation with active PLDδ, but not with catalytically inactive PLDδ. GAPC overexpression enhanced the seedling thermotolerance and the expression of heat‐inducible genes, but this effect was abolished in the pldδ background. Heat stress elevated the levels of the PLD product phosphatidic acid (PA) in the nucleus in wild type, but not in pldδ plants. Lipid labeling demonstrated the heat‐induced nuclear co‐localization of PA and GAPC, which was impaired by zinc, which inhibited the PA–GAPC interaction, and by the membrane trafficking inhibitor brefeldin A (BFA). The GAPC nuclear accumulation and seedling thermotolerance were also decreased by treatment with zinc or BFA. Our data suggest that PLDδ and PA are critical for the heat‐induced nuclear translocation of GAPC. We propose that PLDδ‐produced PA mediates the process via lipid–protein interaction and that the lipid mediation acts as a cellular conduit linking stress perturbations at cell membranes to nuclear functions in plants coping with heat stress. Significance Statement: We found that the plasma membrane‐associated PLDδ and its product phosphatidic acid (PA) mediate heat‐induced nuclear translocation of cytosolic GAPC, and the lipid mediator PA may act as a cellular conduit linking stress perturbations at cell membranes to nuclear functions in plants coping with changing environments. [ABSTRACT FROM AUTHOR]

Summary: Diacylglycerol kinase (DGK) phosphorylates diacylglycerol (DAG) to generate phosphatidic acid (PA), and both DAG and PA are lipid mediators in the cell. Here we show that DGK1 in rice (Oryza sativa) plays important roles in root growth and development.Two independent OsDGK1‐knockout (dgk1) lines exhibited a higher density of lateral roots (LRs) and thinner seminal roots (SRs), whereas OsDGK1‐overexpressing plants displayed a lower LR density and thicker SRs than wild‐type (WT) plants.Overexpression of OsDGK1 led to a decline in the DGK substrate DAG whereas specific PA species decreased in dgk1 roots. Supplementation of DAG to OsDGK1‐overexpressing seedlings restored the LR density and SR thickness whereas application of PA to dgk1 seedlings restored the LR density and SR thickness to those of the WT. In addition, treatment of rice seedlings with the DGK inhibitor R59022 increased the level of DAG and decreased PA, which also restored the root phenotype of OsDGK1‐overexpressing seedlings close to that of the WT.Together, these results indicate that DGK1 and associated lipid mediators modulate rice root architecture; DAG promotes LR formation and suppresses SR growth whereas PA suppresses LR number and promotes SR thickness. [ABSTRACT FROM AUTHOR]

Phosphatidylinositol‐specific phospholipase C (PI‐PLC) is involved in stress signalling but its signalling function remains largely unknown in crop plants. Here, we report that the PI‐PLC4 from rice (Oryza sativacv), OsPLC4, plays a positive role in osmotic stress response. Two independent knockout mutants, plc4‐1 and plc4‐2, exhibited decreased seedling growth and survival rate whereas overexpression of OsPLC4 improved survival rate under high salinity and water deficiency, compared with wild type (WT). OsPLC4 hydrolyses PI, phosphatidylinositol 4‐phosphate (PI4P), and phosphatidylinositol‐4,5‐bisphosphate (PIP2) to generate diacylglycerol (DAG) in vitro. Knockout of OsPLC4 attenuated salt‐induced increase of phosphatidic acid (PA) whereas overexpression of OsPLC4 decreased the level of PI4P and PIP2 under salt treatment. Applications of DAG or PA restored the growth defect of plc4‐1 to WT but DAG kinase inhibitor 1 blocked the complementary effect of DAG in plc4‐1 under salt stress. In addition, the loss of OsPLC4 compromised the increase of inositol triphosphate and free cytoplasmic Ca2+ ([Ca2+]cyt) and inhibited the induction of genes involved in Ca2+ sensor and osmotic stress response to salt stress. The results indicate that OsPLC4 modulates the activity of two signalling pathways, PA and Ca2+, to affect rice seedling response to osmotic stress. Synopsis: High salinity is a major stress challenging rice production. This study showsthat the phosphatidylinositol‐hydrolyzing phospholipase C4 is involved in rice response to NaCl. OsPLC4 modulates the stress response through lipid‐ and Ca2+‐mediated signaling. High salinity is a major stress challenging rice production. This study shows that the phosphatidylinositol‐hydrolyzing phospholipase C4 is involved in rice response to NaCl. OsPLC4 modulates the stress response through lipid‐ and Ca2+‐mediated signalling. [ABSTRACT FROM AUTHOR]

Pathogen infection of higher plants often induces rapid production of phosphatidic acid ( PA) and changes in lipid profiles, but the enzymatic basis and the function of the lipid change in pathogen-plant interactions are not well understood., Infection of phospholipase D β1 ( PLDβ1)-deficient plants by Pseudomonas syringae tomato pv DC3000 ( Pst DC30000) resulted in less bacterial growth than in wild-type plants, and the effect was more profound in virulent Pst DC3000 than avirulent Pst DC3000 (carrying the avirulence gene avrRpt2) infection. The expression levels of salicylic acid ( SA)-inducible genes were higher, but those inducible by jasmonic acid ( JA) showed lower expression in PLDβ1 mutants than in wild-type plants., However, PLDβ1-deficient plants were more susceptible than wild-type plants to the fungus Botrytis cinerea. The PLDβ1-deficient plants had lower levels of PA, JA and JA-related defense gene expression after B. cinerea inoculation., PLDβ1 plays a positive role in pathogen-induced JA production and plant resistance to the necrotrophic fungal pathogen B. cinerea, but a negative role in the SA-dependent signaling pathway and plant tolerance to infection with biotrophic Pst DC3000. PLDβ1 is responsible for most of the increase in PA production in response to necrotrophic B. cinerea and virulent Pst DC3000 infection, but contributes less to avirulent Pst DC3000 ( avrRpt2)-induced PA production. [ABSTRACT FROM AUTHOR]

The activation of phospholipase Dα1 ( PLDα1) produces lipid messenger phosphatidic acid and promotes stomatal closure in Arabidopsis. To explore the use of the PLDα1-mediated signalling towards decreasing water loss in crop plants, we introduced Arabidopsis PLDα1 under the control of a guard cell-specific promoter At Kat I pro into two canola ( Brassica napus) cultivars. Multiple At Kat I pro :: PLDα1 lines in each cultivar displayed decreased water loss and improved biomass accumulation under hyperosmotic stress conditions, including drought and high salinity. Moreover, At Kat I pro :: PLDα1 plants produced more seeds than did WT plants in fields under drought. The results indicate that the guard cell-specific expression of PLDα1 has the potential to improve crop yield by enhancing drought tolerance. [ABSTRACT FROM AUTHOR]

In response to elevated temperatures, plants alter the activities of enzymes that affect lipid composition. While it has long been known that plant leaf membrane lipids become less unsaturated in response to heat, other changes, including polygalactosylation of galactolipids, head group acylation of galactolipids, increases in phosphatidic acid and triacylglycerols, and formation of sterol glucosides and acyl sterol glucosides, have been observed more recently. In this work, by measuring lipid levels with mass spectrometry, we confirm the previously observed changes in Arabidopsis thaliana leaf lipids under three heat stress regimens. Additionally, in response to heat, increased oxidation of the fatty acyl chains of leaf galactolipids, sulfoquinovosyldiacylglycerols, and phosphatidylglycerols, and incorporation of oxidized acyl chains into acylated monogalactosyldiacylglycerols are shown. We also observed increased levels of digalactosylmonoacylglycerols and monogalactosylmonoacylglycerols. The hypothesis that a defect in sterol glycosylation would adversely affect regrowth of plants after a severe heat stress regimen was tested, but differences between wild-type and sterol glycosylation-defective plants were not detected. [ABSTRACT FROM AUTHOR]

Phospholipases D (PLD) and C (PLC) hydrolyze the phosphodiesteric linkages of the head group of membrane phospholipids. PLDs and PLCs in plants occur in different forms: the calcium-dependent phospholipid binding domain-containing PLDs (C2-PLDs), the plekstrin homology and phox homology domain-containing PLDs (PX/PH-PLDs), phosphoinositide-specific PLC (PI-PLC), and non-specific PLC (NPC). They differ in structures, substrate selectivities, cofactor requirements, and/or reaction conditions. These enzymes and their reaction products, such as phosphatidic acid (PA), diacylglycerol (DAG), and inositol polyphosphates, play important, multifaceted roles in plant response to abiotic and biotic stresses. Here, we review biochemical properties, cellular effects, and physiological functions of PLDs and PLCs, particularly in the context of their roles in stress response along with advances made on the role of PA and DAG in cell signaling in plants. The mechanism of actions, including those common and distinguishable among different PLDs and PLCs, will also be discussed. [ABSTRACT FROM AUTHOR]