3.1.4.4 DNA + H2O endonuclease 3.1.4.4 additional information involved in wound-induced metabolism of polyunsaturated fatty acids 3.1.4.4 additional information PldA contributes to the ability of Pseudomonas aeruginosa PAO1 to persist in a chronic pulmonary infection model in rats 3.1.4.4 additional information 5-[4-acridin-[9-ylamino]phenyl]-5-methyl-3-methylenedihydrofuran-2-one inhibits the formyl-Met-Leu-Phe-stimulated phospholipase D activity, mainly through the blockade of RhoA activation and degranulation 3.1.4.4 additional information activation of phospholipase D by 8-Br-cAMP occurs through a pathway involving Src, Ras, and ERK in human endometrial stromal cells 3.1.4.4 additional information alpha-adrenoreceptor activation increases phospholipase D activity 3.1.4.4 additional information constitutive cation channel activity in ear artery myocytes is mediated by diacylglycerol which is generated by phosphatidylcholine-phospholipase D via phosphatidic acid which represents a novel activation pathway of cation channels in vascular myocytes 3.1.4.4 additional information crosstalk between protein kinase A and C regulates phospholipase D and F-actin formation during sperm capacitation 3.1.4.4 additional information dependency of activation of protein kinase D on phospholipase D, phospholipase D could be a key molecule that links Rho/protein kinase C signaling to diacylglycerol for protein kinase D activation 3.1.4.4 additional information down-regulation of melanogenesis is mediated by phospholipase D2 but not by phospholipase D1 through turbiquitin proteasome-mediated degradation of tyrosinase. PLD2 may play an important role in regulating pigmentation in vivo 3.1.4.4 additional information essential role for phospholipase D in activation of protein kinase C and degranulation in mast cells. Production of phosphatidic acid by PLD facilitates activation of protein kinase C and, in turn, degranulation, although additional PLD-dependent processes appear to be critical for antigen-mediated degranulation 3.1.4.4 additional information expression of LePLDbeta1 is increased upon treatment with xylanase. Possible involvement of LePLDbeta1 in plant defense response 3.1.4.4 additional information increase in local membrane monomeric tubulin concentration inhibits PLD2 activity. The PLD2 regulating mechanism via tubulin exists in endogeneous muscarinic receptor possessing cells 3.1.4.4 additional information interaction of the PLD1 PX domain with phosphatidylinositol 3,4,5-trisphosphate and/or phosphatidic acid (or phosphatidylserine) may be an important factor in the spatiotemporal regulation and activation of PLD1 3.1.4.4 additional information lysophosphatidic acid activates protein translation through the action of PLD1-generated phosphatidic acid on mTOR and the phosphoinositide 3-kinase/Akt pathway 3.1.4.4 additional information lysophosphatidic acid increases phospholipase D activity in neutrophils 3.1.4.4 additional information mechanical stimuli activate mTOR (mammalian target of rapamycin) signaling through a phospholipase D-dependent increase in phosphatidic acid 3.1.4.4 additional information Munc-18-1 is a potent negative regulator of basal PLD activity. EGF stimulation abolishes this interaction 3.1.4.4 additional information Peanut PLD may be involved in drought sensitivity and tolerance responses. PLD gene expression is induced faster by drought stress in the drought-sensitive lines than in the drought tolerant lines. Cultivated peanut has multiple copies (3 to 5 copies) of the PLD gene 3.1.4.4 additional information phorbol 12-myristate 13-acetate induces PLD2 activation via the involvement of protein kinase Calpha. PLD2 becomes phosphorylated on both Ser and Thr residues. Interaction rather than phosphorylation underscores the activation of PLD2 by protein kinase Calpha in vivo. Phosphorylation may contribute to the inactivation of the enzyme 3.1.4.4 additional information phospholipase D activity is essential for actin localization and actin-based motility 3.1.4.4 additional information phospholipase D alpha is a key enzyme involved in membrane deterioration that occurs during fruit ripening and senescence 3.1.4.4 additional information phospholipase D elevates the level of MDM2 and suppresses DNA damage-induced increase in p53 3.1.4.4 additional information phospholipase D facilitates phototransduction by maintaining adequate levels of phosphatidylinositol 4,5-bisphosphate and by protecting the visual system from metarhodopsin-induced, low light degeneration 3.1.4.4 additional information phospholipase D plays an important role in the regulation of beta-hexosaminidase release in actively sensitized rat peritoneal mast cells 3.1.4.4 additional information PLD activity is constitutive during pollen tube growth. Hypoosmotic stress stimulates PLD activity, hyperosmotic stress attenuates PLD activity 3.1.4.4 additional information PLD is activated by H2O2. The activation by H2O2 enhances phytoalexin biosynthesis in rice cells 3.1.4.4 additional information PLD is actived by the chemotactic peptide N-formyl-methionyl-leucyl-phenylalanine. PLD2, but not PLD1, contributes to PLD activity mediated by N-formyl-methionyl-leucyl-phenylalanine. Extracellular signal-regulated kinase/PLD2 pathway contributes to N-formyl-methionyl-leucyl-phenylalanine-mediated oxidant production 3.1.4.4 additional information PLD might be implicated in core protein-induced transformation 3.1.4.4 additional information PLD1 is a signaling node, in which integration of convergent signals occurs within discrete locales of the cellular membrane 3.1.4.4 additional information PLD1 is required for normal organization of the actin cytoskeleton and for cell motility. PLD1 is a critical factor in the organization of the actin-based cytoskeleton, with regard to cell adhesion and migration 3.1.4.4 additional information PLD1 plays a role in the induction of gene expression of Cox-2 and IL-8 3.1.4.4 additional information PLD2 may be involved in early developmental processes of some neuronal progenitors 3.1.4.4 additional information priming is a critical regulator of PLD activation 3.1.4.4 additional information prolonged elevation of PLD activity is required for myogenic differentiation 3.1.4.4 additional information protein casein kinase II stimulates basal phospholipase D (PLD1 and PLD2) activity as well as PMA-induced phospholipase D activation in human U87 astroglioma cells 3.1.4.4 additional information regulation of phospholipase D activity by light and phytohormones. abscisic acid manifests a short-term stimulating effect on phospholipase D activity in the green seedlings and inhibits phospholipase D activity in the etiolated plants. Kinetin inhibits enzyme activity in the etiolated seedlings and does not affect its activity in light. gibberellic acid does not markedly affect phospholipase D activity in the etiolated plant and activates this enzyme in the green seedling 3.1.4.4 additional information sphingosine significantly stimulates phospholipase D activity in mouse C2c12 myoblasts via phosphorylation to sphingosine 1-phosphate 3.1.4.4 additional information stimulation of PLD activity and its mRNA expression by lipopolysaccharides might be required for IL-2 R expression and a sustained PKC dependent intracellular pH elevation but not for secretion of IL-2 or IL-4 in T cells 3.1.4.4 additional information survival signals generated by PLD attenuate expression of Egr-1 by activation of phosphatidylinositol 3-kinase signaling pathway and induction of PTEN by early growth response-1, which confers resistance to apoptosis 3.1.4.4 additional information the Arf-GTPase-activating protein Gsc1p is essential for sporulation and positively regulates the phospholipase D Spo14p 3.1.4.4 additional information the enzyme participates in myogenesis through phosphatidic acid- and phosphatidylinositol bisphosphate-dependent actin fiber formation 3.1.4.4 additional information the enzyme plays an essential role in the swelling-induced vesicle cycling and in the activation of volume-sensitive anion channels 3.1.4.4 additional information the PLD gene undergoes qualitative changes in transcription regulation during granulocytic differentiation 3.1.4.4 additional information the PLD2 PX domain enables PLD1 to mediate signal transduction via ERK1/2 by providing a direct binding site for phosphatidylinositol 3,4,5-triphosphate and by activating PLD1 3.1.4.4 additional information thyrotrophin-releasing hormone increases phospholipase D activity through stimulation of protein kinase C in GH3 cells 3.1.4.4 additional information vitamin C at pharmacological doses activates PLD in the lung microvascular endothelial cells through oxidative stress and activation of mitogen-activated protein kinase 3.1.4.4 additional information white and red light exposure inhibits enzyme activity in etiolated seedlings. Phospholipase D activity is regulated by light with involvement of phytochrome photoreceptor and associated with photosynthesis process 3.1.4.4 additional information endocytotic trafficking of my-opioid receptor MOR1, delta-opioid receptor DOR and cannabinoid receptor isoform CB1 are mediated by an isoform PLD2 dependent pathway 3.1.4.4 additional information enzyme augments gonococcus invasion of cervical epithelia by interacting with Akt kinase in a hosphatidylinositol-(3,4,5)-trisphosphate-independent manner, resulting in subversion of normal cervical cell signaling 3.1.4.4 additional information enzyme evokes inflammatory reactions following injections into rabbit skin. Enzyme has a small hemolytic effect 3.1.4.4 additional information enzyme evokes inflammatory reactions following injections into rabbit skin. Treatment of Madin-Darby canine kidney cells results in appearance of cytoplasmic vacuolization, altered cellular spreading and cell-cell adhesion. Enzyme causes a high degree of hemolysis 3.1.4.4 additional information enzyme is activated downstream of ERK1/2 kinases upon chemokine receptor CCR5 activation and plays a major role in promoting HIV-1 LTR transactivation and virus replication 3.1.4.4 additional information enzyme is required for cellularization, i.e. A form of cytokinesis in which polarized membrane extension proceeds in part through incorporation of new membrane via fusion of apically-translocated Golgi-derived vesicles. Loss of enzyme activity frequently leads to early embryonic developmental arrest 3.1.4.4 additional information enzyme isoform PLD1 and PLD2 are closely related with Bcl-2 expression together with phospholipase A2, but not with phosphatidic acid phosphohydrolase, during taxotere-induced apoptosis in SNU 484 cells 3.1.4.4 additional information enzyme shows dermonbecrotic properties. Enzyme causes massive inflammatory response in rabbit skin dermis, evokes platelet aggregation, increases vascular permeability, causes edema and death in mice 3.1.4.4 additional information hydrolysis of phosphatidylcholine by enzyme isoforms PLDzeta1 and PLDzeta2 during phosphorus starvation contributes to the supply of inorganic phosphorus for cell metabolism and diacylglycerol moieties for galactolipid synthesis 3.1.4.4 additional information isoform PLD1 isassociated with cell polarity and directionality concomitantly with adhesion and F-actin polymerization in response to IL-8 3.1.4.4 additional information isoform PLD1 plays a crucial role in collagen type I production through mTOR signaling in dermal fibroblast 3.1.4.4 additional information isoform PLD2 is associated with cell polarity and directionality concomitantly with adhesion and F-actin polymerization in response to IL-8 3.1.4.4 additional information isoform PLDbeta1 stimulates abscisic acid signaling by activating SAP kinase, thus repressing GAmyb expression and inhibiting seed germination 3.1.4.4 additional information mechanical stimuli activate signaling by mTOR, i.e. mammalian target of rapamycin, in skeletal muscle through an enzyme-dependent increase in phosphatidic acid 3.1.4.4 additional information phospholipase D functions as a GTPase activating protein through the phox homology domain, which directly activates the GTPase domain of dynamin. Enzyme increases epidermal growth factor receptor endocytosis at physiological concentrations of epidermal growth factor 3.1.4.4 additional information up-regulation of beta-defensin-2 by cell wall extract of Fusobacterium nucleatum or phorbol 12-myristate 13-acetate is mediated by phospholipase D 3.1.4.4 additional information incubation of Arabidopsis thaliana cell suspensions with primary alcohols inhibit the induction of two salicylic acid-responsive genes, PR1 and WRKY38, in a dose dependent manner. This inhibitory effect is more pronounced when the primary alcohols are more hydrophobic. Secondary or tertiary alcohols have no inhibitory effect. These results show that PLD activity is upstream of the induction of these genes by salicylic acid. A detailed analysis of the regulation of salicylic acid-responsive genes show that PLD can act both positively and negatively, either on gene induction or gene repression 3.1.4.4 additional information PLD product phosphatidic acid acts as a membrane anchor of Rac1. The C-terminal polybasic motif of Rac1 is responsible for direct interaction with phosphatidic acid. It is shown that phosphatidic acid induces dissociation of Rho-guanine nucleotide dissociation inhibitor from Rac1 and that phosphatidic acid-mediated Rac1 localization is important for integrin-mediated lamellipodia formation, cell spreading, and migration 3.1.4.4 additional information PLD product phosphatidic acid acts as a membrane anchor of Rac1. The C-terminal polybasic motif of Rac1 is responsible for direct interaction with phosphatidic acid. Phosphatidic acid induces dissociation of Rho-guanine nucleotide dissociation inhibitor from Rac1 and that phosphatidic acid-mediated Rac1 localization is important for integrin-mediated lamellipodia formation, cell spreading, and migration 3.1.4.4 additional information ability of PLD-generated phosphatidic acid to control actin polymerization and the reciprocal ability of actin to specifically modulate PIP2-dependent PLD, PLDbeta, activity through direct interaction 3.1.4.4 additional information effects of active and inactive phospholipase D2 on signal transduction, adhesion, migration, invasion, and metastasis in EL4 lymphoma cells, overview 3.1.4.4 additional information isozymes PLD1 and PLD2 share aboout 50% homology, but are regulated and localized differently in the cell. In vitro, PLD2 has a higher basal activity than PLD1, but overall cellular activity of PLD is low 3.1.4.4 additional information NF-kappaB and transcription factor Sp1 are essential transcriptional factors linking PLD to MMP-2 upregulation 3.1.4.4 additional information phospholipase D activates native TRPC3 cation channels after stimulation of G-protein-coupled type I glutamate receptors in the cerebellum. Small GTPases might be involved in the activation mechanism of TRPC3 in rat cerebellar Purkinje cells, overview 3.1.4.4 additional information PLD also performs transphosphatidylation using 1-butanol as phosphatidyl acceptor 3.1.4.4 additional information PLD also performs transphosphatidylation using 1-butanol as phosphatidyl acceptor, the transphosphatidylation reaction is an index of PLD activity in intact cells 3.1.4.4 additional information PLD catalyzes the hydrolysis of phospholipids resulting in the generation of phosphatidic acid and the release of the polar head group. The enzyme also catalyzes a transphosphatidylation reaction, in which the aliphatic chain of the primary alcohol is transferred to the phosphatidyl moiety of the phosphatidic acid product 3.1.4.4 additional information PLD isozymes are cleaved by caspase 3, cleavage site determination, isozyme PLD2alpha contains two consensus motifs for caspase 3 cleavage, DXXD or D/E, D/E, X, D, located in the loop region at DDVD545S between the PLD domains, mutational analysis, overview 3.1.4.4 additional information PLD isozymes are cleaved by caspase 3, cleavage site determination, isozymes PLD1beta and PLD2alpha contain each two consensus motifs for caspase 3 cleavage, DXXD or D/E, D/E, X, D, located in the loop region at DDVD545S and DFID631R between the PLD domains, respectively, mutational analysis, overview 3.1.4.4 additional information PLD performs two different reactions: a hydrolytic reaction and a transphosphatidylation reaction, 1-butanol serves as acceptor in the transphosphatidylation reaction, while 2-butanol does not. PLD-catalysed PtdOH formation may be necessary for EGF-induced macropinocytosis 3.1.4.4 additional information PLD performs two different reactions: a hydrolytic reaction and a transphosphatidylation reaction, the latter with a primary alcohol, both pathway share a common intermediate, mechanism, overview 3.1.4.4 additional information PLD1 mediates the reactive oxygen species-induced increase in diacylglycerol, which facilitates PKD1 localization to the mitochondria and its activation. Diacylglycerol, to which PKD1 is recruited, is formed downstream of phospholipase D1 and is required for PKD1 localization in the mitochondria and well as activation under oxidative stress, overview. Role for PLD1-induced DAG as a competent second messenger at the mitochondria that relays ROS to PKD1-mediated mitochondria-to-nucleus signaling 3.1.4.4 additional information PLD2 is regulated by phosphorylation-dephosphorylation, detailed overview 3.1.4.4 additional information PLDalpha1 interacts with the Galpha1 subunit of the heterotrimeric G protein to inhibit stomatal opening 3.1.4.4 additional information silymarin secretion and its elicitation by methyl jasmonate in cell cultures of Silybum marianum is mediated by phospholipase D-phosphatidic acid, overview 3.1.4.4 additional information the different PLDs exhibit distinguishable reaction conditions, substrate preferences and subcellular localization, overview. PLDalpha1 interacts with Galpha protein, a heterotrimeric Galpha protein to prevent closed stomata from opening 3.1.4.4 additional information interaction of PLDalpha C2 domain with synthetic unilamellar vesicles shows maximum affinity towards phosphatidic acid, and virtually no binding with phosphatidylcholine. Electrostatic, rather than a hydrophobic mode of interaction between C2 domain and the phospholipid vesicles. The binding towards phosphoinositides is reduced with increasing degree of phosphorylation 3.1.4.4 additional information purified PLDalpha is inactive in vitro on bilamellar substrates. It is fully active on mixed micelles made with phospholipids and a mixture of Triton-X100 and SDS at equal concentrations. Ca2+ interacts with the SDS contained in the mixed micelles thus leading to an aggregated form of the substrate which is more easily hydrolyzed by PLDalpha 3.1.4.4 phosphatidylcholine + H2O both phosphatidylcholine and phosphatidylethanolamine are substrates for phospholipase D in UMR-106 osteoblastic cells and can therefore be sources of phospholipid hydrolysis products for downstream signaling in osteoblast 3.1.4.4 phosphatidylcholine + H2O - 3.1.4.4 phosphatidylcholine + H2O Regulation and effectors of phospholipase D and phosphatidic acid on the Golgi apparatus, overview 3.1.4.4 phosphatidylcholine + H2O hydrolysis of phosphatidylcholine by phospholipase D leads to the generation of phosphatidic acid, PA, which is itself a source of diacylglycerol. PLD2 emerges as an early player upstream of the Ras-MAPK-IL-2 pathway in T-cells via PA and DAG production 3.1.4.4 phosphatidylcholine + H2O hydrolysis of phosphatidylcholine by phospholipase D leads to the generation of phosphatidic acid, which is itself a source of diacylglycerol. PLD2 emerges as an early player upstream of the Ras-MAPK-IL-2 pathway in T-cells via phosphatidic acid and diacylglycerol production 3.1.4.4 phosphatidylcholine + H2O phosphatidic acid activates the production of and promotes accumulation of silymarin, overview 3.1.4.4 phosphatidylethanolamine + H2O parathyroid hormone stimulates phosphatidylethanolamine hydrolysis by phospholipase D in osteoblastic cells. Both phosphatidylcholine and phosphatidylethanolamine are substrates for phospholipase D in UMR-106 osteoblastic cells and can therefore be sources of phospholipid hydrolysis products for downstream signaling in osteoblast 3.1.4.4 phosphatidylethanolamine + H2O - 3.1.4.4 phosphatidylglycerol + H2O - 3.1.4.4 phosphatidylserine + H2O - 3.1.4.4 phospholipid + alcohol transphosphaditylation 3.1.4.4 phospholipid + H2O phosphoric ester hydrolysis