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malfunction
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catalytically deficient FLAG-tagged H223L LPP1 mutant can form an oligomer with wild-type LPP1, whereby wild-type LPP1 activity is preserved in the oligomer
malfunction
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deletion of PAH1 leads to the accumulation of phosphatidic acid but also the concomitant reduction of 1,2-diacyl-sn-glycerol and triacylglycerol levels and changes in phosphatidylethanolamine and phosphatidylcholine amounts. Mammalian lipins can rescue the yeast pah1DELTA mutant. A septuple S/T-P Pah1p phosphorylation null mutant displays higher specific activity when compared to the wild-type enzyme. Mutations in Pah1p result in transcriptional derepression of UAS(INO)-containing genes. Overexpression of the more active septuple S/T-P Pah1p phosphorylation null mutant causes inositol auxotrophy, which can be rescued by the deletion of the Opi1p repressor. Pah1DELtAopi1DELTA double mutant exhibits a synergistic effect on the transcriptional derepression of two UAS(INO)-containing genes, INO1 and OPI3. PAH1 mutants display irregularly shaped nuclei with long stacks of membranes that contain nuclear pores and appear to be in contact with the nuclear envelope. Inactivation of the phosphatidic acid signals downstream of Pah1p by either deleting the transcriptional activator Ino2p or overexpressing the repressor Opi1p, can restore normal nuclear shape in nem1DELTA spo7DELTA or pah1DELTA deletion mutants
malfunction
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depletion of LPP3 results in destabilization of beta-catenin, which in turn reduces fibronectin synthesis and deposition, which results in inhibition of endothelial cell migration. Reexpression of beta-catenin but not p120-catenin in LPP3-depleted endothelial cells restores de novo synthesis of fibronectin, which mediates endothelial cell migration and formation of branching point structures. LPP3-RAD mutant, which is defective for integrin binding and a LPP3-PD mutant, which is defective for phosphatase activity stimulate lymphoid enhancer binding factor 1-dependent transcription 3- or 5fold, respectively. The LPP3 mutant that lacks both adhesion and lipid phosphatase domains (hLPP3-RAD+PD) fails to stimulate luciferase activity
malfunction
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double mutant pah1pah2 plants have decreased phosphatidic acid hydrolysis, thus affecting the eukaryotic pathway of galactolipid synthesis. Upon phosphate starvation, pah1pah2 plants are severely impaired in growth and membrane lipid remodeling. PAP activity in the supernatant fraction of pah1pah2 mutant leaves is decreased by approximately 40% as compared to that in wild-type leaves. Defect in PAP activity in vivo in rosette leaves of pah1pah2 mutants. Relative amount of phosphatidic acid increases to 1.61fold in pah1pah2 double mutants as compared to the wild-type. 26% increase in phosphatidic acid levels in pah1pah2 plants as compared to wild-type plants. The transgenic plants (35S::PAH1-GFP, pah1pah2 and 35S::PAH2-GFP, pah1pah2) recover the phenotype observed in pah1pah2 mutant. Endoplasmic reticulum-localized eukaryotic pathway of membrane lipid metabolism is compromised in pah1pah2 double mutants
malfunction
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downregulating LPIN-1 by RNAi results in the appearance of membrane sheets and other abnormal structures in the peripheral endoplasmic reticulum. Lpin-1 RNAi causes defects in nuclear envelope breakdown, abnormal chromosome segregation and irregular nuclear morphology. RNAi of lipin results in reduced body size and defects in lipid storage
malfunction
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in fat pads from mice deficient for lipin 1 (fld mice) and in 3T3-L1 adipocytes depleted of lipin 1 there is increased expression of several nuclear factor of activated T-cells target genes including TNFalpha, resistin, FABP4 and PPARgamma. Lipin 1 with the highly conserved amino-terminal NLIP domain deleted (DELTAN) is capable of both interaction and repression
malfunction
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in mutants where both Wun and wun2 are disrupted, germ cells scatter throughout the embryo and eventually die
malfunction
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knockdown of endogenous lipin-1 expression decreases the secretion of newly synthesized triglycerides
malfunction
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lipin 1 deficiency does not affect PAP-1 activity in neonatal mice and leads to hepatic triglyceride accumulation. Loss of lipin 2 markedly impairs hepatocyte PAP-1 activity but does not affect basal rates of triglyceride synthesis. Lipin 2 knockdown abrogates triglyceride synthesis under conditions of increased fatty acid availability
malfunction
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lipin 1 gene is mutated in the fatty liver dystrophy mouse, which displays features of generalized lipodystrophy, characterized by significant reduction in the adipose tissue mass and in the cellular lipid droplet content
malfunction
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lipin-1 deficiency causes lipodystrophy, neonatal fatty liver, peripheral neuropathy, insulin resistance, and increased susceptibility to atherosclerosis
malfunction
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lipin-1 deficiency in rare human patients, causes acute myoglobinuria in childhood, does not result in lipodystrophy in these individuals. Muscle sample from a patient with lipin-1 deficiency reveals elevated phosphatidate levels. Rare patients with lipin-2 deficiency have a complex phenotype known as Majeed syndrome, characterized by recurrent osteomyelitis, fever, and anemia
malfunction
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lipin-1 deficiency produces lipodystrophy. In fatty liver dystrophy mice, occurrence of fatty liver and hypertriglyceridemia during the neonatal period, and peripheral neuropathy, which progresses throughout adulthood. Fatty liver dystrophy mice are lipodystrophic, develop insulin resistance, and have increased susceptibility to atherosclerosis. Lipin-2 cannot compensate for lipin-1 function in adipose tissue of fatty liver dystrophy mice
malfunction
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LPP1 hypomorph mice (Ppap2atr/tr) have depleted LPP1 expression in most tissues. Lysophosphatidate concentrations in the plasma are higher in Ppap2atr/tr mice compared with controls. Embryos from LPP3 knockout mice fail to form a chorio-allantoic placenta and yolk sac vasculature and some embryos show shortening of the anterior-posterior axis similar to axin deficiency, a critical regulator of Wnt signaling. LPP2 knockout mice are fertile and viable with no obvious phenotype
malfunction
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mutations affecting lipin-1 and lipin-2 cause human disease. Human lipodystrophic subjects do not show causative mutations in the LPIN1 gene. Mutations in LPIN1 in patients with recurrent acute myoglobinuria in childhood. Distinct inactivating mutations in patients from several ethnic backgrounds and at dispersed locations throughout the lipin-1 protein structure. LPIN1 polymorphisms are associated with numerous metabolic traits, like insulin and/or glucose levels, resting metabolic rate, and systolic blood pressure. LPIN1 polymorphisms associated with response of type 2 diabetic patients to rosiglitazone. LPIN1 polymorphism can cause an amino acid substitution within the C-LIP domain, which is associated with statin-induced myopathy
malfunction
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nuclear localization is abrogated by mutating the consensus sumyolation motifs. Sumoylation site mutant of lipin-1alpha loses the capacity to coactivate the transcriptional (co-) activators PGC-1alpha and MEF2, consistent with its nuclear exclusion
malfunction
RNAi downregulation of lpin-1 for 48 hours or longer results in 100% embryonic lethality on N2 worms. Inactivation of lpin-1 promotes bi-nucleation. Co-depletion of lpin-1 and lamin significantly rescues the effect of lpin-1 depletion on nuclear envelope breakdown
malfunction
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symptoms of the Majeed syndrome result from a loss of lipin-2 PAP activity. Loss of lipin-2 PAP activity in erythrocytes and lymphocytes may contribute to the anemia and inflammation phenotypes observed in Majeed syndrome patients
malfunction
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yeast DELTAdpp1DELTAlpp1DELTApah1 mutant is complemented by Arabidopsis phosphatidate phosphatases PAH1 and PAH2 in vivo
malfunction
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cells lacking phosphatidate phosphatase are sensitive to exogenous fatty acids in the order of toxicity palmitoleic acid > oleic acid > palmitic acid
malfunction
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fatty liver dystrophy mice carrying mutations within the lipin 1 gene display life-long deficiency in adipogenesis, insulin resistance, neonatal hepatosteatosis and hypertriglyceridemia, as well as increased atherosclerosis susceptibility. Lipin-1 deficiency results in the activation of the sterol regulatory element binding protein 1 and its target genes as well as in very high expression levels of stearoyl-CoA desaturase-1 and apoA-IV. Acute lipin-1 deficiency in the mouse liver abolishes fasting-induced activation of Ppara and several PPARalpha/PGC-1alpha target genes, such as Acadvl, Acadm and Fabp1
malfunction
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lack of wun2 in germ cells results in germ cell death
malfunction
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lipid phosphate phosphatase-3-knockdown inhibits both U-87 and U-118 glioblastoma cell proliferation in culture and tumor growth in xenograft assays. Lipid phosphate phosphatase-3-knockdown reduces beta-catenin, cyclin-D1, and CD133 expression, with a concomitant increase in phosphorylated beta-catenin
malfunction
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lipin-1 deficiency in humans is not associated with lipodystrophy. In HeLa cells, knockdown of lipin-2 results in increased phosphatidate phosphatase activity, apparently as a result of compensatory upregulation of lipin-1
malfunction
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partitioning of substrate between the prokaryotic and eukaryotic pathways is perturbed in the pah1 pah2-1 double mutant. Both the total lipid content and the phospholipid content of pah1 pah2-1 mutant leaves and roots is greater than wild type on a per unit fresh weight basis
malfunction
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the inhibition of stomatal opening is less sensitive to abscisic acid in lipid phosphate phosphatase 2-deficient plants than in wild type plants. Lipid phosphate phosphatase 2-deficient plants accumulate more phosphatidic acid than wild type and have a higher phosphatidic acid kinase activity
malfunction
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cell death-inducing stresses are required for defense activation in DS1-phosphatidic acid phosphatase-silenced Nicotiana benthamiana
malfunction
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enzyme deletion causes multiple phenotypes, especially severe hyphal defects, increased sensitivity to cell wall stress, and reduced virulence in mice
malfunction
LPP3 deficiency, specifically targeted at vascular cell types, induces endothelial permeability, promotes leukocyte adhesion to endothelial cells and stimulates smooth muscle cell proliferation. Hepatocyte-specific Plpp3 deficiency, by modulating the plasma lipidome, exacerbates atherosclerosis development in Apoe-/-x01mice
malfunction
LPP3 deficiency, specifically targeted at vascular cell types, induces endothelial permeability, promotes leukocyte adhesion to endothelial cells, and stimulates smooth muscle cell proliferation
malfunction
LPP3 silencing in human primary aortic endothelial cells enhances secretion of inflammatory cytokines, leucocyte adhesion, cell survival, and migration and impairs angiogenesis, whereas wild-type LPP3 overexpression reversed these effects and induces apoptosis
malfunction
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cells lacking phosphatidate phosphatase are sensitive to exogenous fatty acids in the order of toxicity palmitoleic acid > oleic acid > palmitic acid
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metabolism
isoform lipin-1 binds to serine/threonine protein phosphatase-1 catalytic subunit through a HVRF binding motif. Mutating the HVRF motif in the highly conserved N terminus of lipin-1 greatly decreases serine/threonine protein phosphatase-1 catalytic subunit interaction. Mutations of other residues in the N terminus of lipin-1 also modulate serine/threonine protein phosphatase-1 catalytic subunit binding. Serine/threonine protein phosphatase-1 catalytic subuni binds poorly to a phosphomimetic mutant of lipin-1 andbinds well to the non-phosphorylatable lipin-1 mutant. Mutating the HVRFmotif also abrogates the nuclear translocation and phosphatidate phosphatase activity of lipin-1
metabolism
isoform Pah1p is a bona fide substrate of protein kinase C. The phosphorylation reaction is time- and dose-dependent and dependent on the concentrations of ATP and Pah1p. The stoichiometry of the reaction is 0.8 mol of phosphate/mol of Pah1p. Unlike its phosphorylations by Pho85p-Pho80p and protein kinase A, which cause a significant reduction in phosphatidate phosphatase activity, the phosphorylation of Pah1p by protein kinase C has a small stimulatory effect on the enzyme activity. Protein kinase C does not have a major effect on Pah1p location or its function in triacylglycerol synthesis
metabolism
isoform Pah1p is stabilized in mutants with impaired proteasome and ubiquitination functions. The pre1 pre2 mutations that eliminate nearly all chymotrypsin-like activity of the 20 S proteasome have the greatest stabilizing effect on enzyme levels. Alteration in phosphatidate and/or diacylglycerol levels might be the signal that triggers Pah1p degradation
metabolism
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target of rapamycin complex TORC1 inhibits the function of phosphatidate phosphatase Pah1, to prevent the accumulation of triacylglycerol. TORC1 regulates Pah1 in part indirectly by controlling the phosphorylation status of Nem1 within the Pah1-activating, heterodimeric Nem1-Spo7 protein phosphatase module
metabolism
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the activity of the enzyme controls the expression of phosphatidylserine synthase for membrane phospholipid synthesis
metabolism
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the enzyme is involved in triacylglycerol biosynthesis during lipogenesis
metabolism
the enzyme plays a major role in controlling the utilization of phosphatidate for the synthesis of triacylglycerol or membrane phospholipids
metabolism
the enzyme regulates phosphatidylcholine biosynthesis in Arabidopsis by phosphatidic acid-mediated activation of CTP:phosphocholine cytidylyltransferase activity
metabolism
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the enzyme is involved in triacylglycerol biosynthesis during lipogenesis
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metabolism
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the activity of the enzyme controls the expression of phosphatidylserine synthase for membrane phospholipid synthesis
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metabolism
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the enzyme plays a major role in controlling the utilization of phosphatidate for the synthesis of triacylglycerol or membrane phospholipids
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physiological function
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activation of fibroblasts by lysophosphatidate causes a translocation of Mg2+-dependent PAP activity to the membrane fraction within 2 min when the production of phosphatidic acid and diacylglycerol is increased by lysophosphatidate and platelet-derived growth factor. Translocations of PAP1 activity probably results from the increased presence of phosphatidic acid in membranes
physiological function
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decreases the growth, survival, and tumorigenesis of ovarian cancer cells. LPP3 contains an exposed arginine-glycine-aspartate (RGD) cell adhesion sequence. LPP3 expression increases cell/cell interactions through alphavbeta3 and anti-alpha5beta1 integrins. LPP1 regulates lysophosphatidic acid-induced calcium release, NF-kappaB activation and interleukin-8 secretion in human bronchial epithelial cells
physiological function
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dimerization of LPP is not required for biological activity. Wun and wun2 act redundantly in germ cells as repellant factors that guide migrating germ cells in embryos. Overexpression of wun or wun2 in somatic tissues causes germ cell repulsion and death
physiological function
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ectopic expression of lipin-1 in L6 myotube increases carnitine palmitoyltransferase-1 and delta-aminolevulinate synthase gene expression
physiological function
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endogenous 14-3-3 proteins interact with lipin-1alpha in HEK293 cells, overexpression of 14-3-3 promotes the cytoplasmic localization of lipin-1 in 3T3-L1 adipocytes. Effect of 14-3-3 is mediated through a serine-rich domain in lipin-1. Insulin stimulates interaction with 14-3-3 and cytoplasmic localization of lipin-1alpha in 3T3-L1 adipocytes
physiological function
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endogenous LPP2 and LPP3 form a complex. Endogenous LPP2 and LPP3 form homo- and hetero-oligomers, which differ in their subcellular localization and which may confer differing spatial regulation of phosphatidic acid and sphingosine 1-phosphate signalling
physiological function
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enhanced expression of lipin-1 in a hepatocyte cell line leads to stimulation of triglyceride synthesis and secretion
physiological function
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enhanced expression of lipin-1 is involved in exercise-induced mitochondrial enzyme adaptations, possibly through 5'-AMP-activated protein kinase- and beta2-adrenergic receptor-related mechanisms
physiological function
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has essential roles in lipid droplet and phospholipid metabolism
physiological function
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has essential roles in lipid droplet and phospholipid metabolism. Pah1p and its regulators are required for the maintenance of a spherical nuclear shape. Pah1p carries an acidic stretch at the C-terminal end. PAH1/SMP2 are independently identified as a dosage suppressor of the spo7DELTA and nem1DELTA deletions. Pah1p has a key signalling function in the transcriptional regulation of genes encoding phospholipid biosynthetic enzymes. Pah1p may have roles in the biogenesis of membrane-bound organelles
physiological function
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key role for lipin-1 in adipocyte differentiation and lipid biosynthesis
physiological function
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key role for LPP3 in orchestrating phosphatase and tensin-mediated beta-catenin/lymphoid enhancer binding factor 1 signaling in endothelial cell migration, cell-cell adhesion, and formation of branching point structures. In subconfluent endothelial cells, LPP3 induces expression of fibronectin via beta-catenin/lymphoid enhancer binding factor 1 signaling in a phosphatase and tensin homologue-dependent manner. In confluent endothelial cells, depletion of p120-catenin restores LPP3-mediated beta-catenin/lymphoid enhancer binding factor 1 signaling. In confluent endothelial cells, depletion of p120-catenin restores LPP3-mediated beta-catenin/lymphoid enhancer binding factor 1 signaling. C-terminal domain of LPP3 regulates the expression of p120ctn and VE-cadherin as well as formation of branching point structures. LPP1 and LPP2 have no effect on luciferase (lymphoid enhancer binding factor 1) activity, whereas LPP3 yields an 9fold increase in luciferase activity. LPP1 and LPP2 show no change in basal phosphorylation of beta-catenin
physiological function
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lipin 1 is a potentially important link between triacylglycerol synthesis and adipose tissue inflammation. Lipin 1 represses nuclear factor of activated T-cells c4 transcriptional activity through protein-protein interaction and in the context of at least two different composite elements. Specific residues required for interaction with lipin 1 are contained within the RHD/DNA binding domain and carboxy terminus of nuclear factor of activated T-cells c4. Lipin 1 is present at the promoters of nuclear factor of activated T-cells c4 transcriptional targets in vivo. Lipin 1 protein and total PAP activity are decreased with increasing adiposity in the visceral, but not subcutaneous, fat pads of ob/ob mice. Lipin 1 can act to repress or activate transcription factors. Lipin 1 interacts with nuclear factor of activated T-cells c4 bound to DNA and is present at the promoters of nuclear factor of activated T-cells target genes. Lipin 1 recruits a histone deacetylase to repress nuclear factor of activated T-cells c4 transcription
physiological function
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lipin 1 may play a role in blood pressure regulation, especially in men. The minor allele of rs10495584 is nominally associated with lower mean systolic and diastolic blood pressures in men, but not in women
physiological function
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lipin 1beta appears to be involved in the pathogenesis of insulin resistance in polycystic ovary syndrome
physiological function
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lipin 2 plays an important role as a hepatic PAP-1 enzyme. Lipin 2 overexpression increases PAP-1 activity in HepG2 cells. Increased hepatic expression of lipin 2 plays a role in increased hepatic triglyceride synthesis rates in ob/ob mice
physiological function
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lipin is needed for lipid storage and development. Lipin activity is needed for normal nuclear structure in dividing cells
physiological function
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lipin proteins serve an important role in regulating the balance of lipid intermediates, including phosphatidic acid and diacylglycerol, and maintenance of cellular lipid homeostasis
physiological function
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lipin-1 accounts for all of the PAP activity in adipose tissue and skeletal muscle, but only part of the activity in liver, heart, kidney, and brain. Enhanced lipin-1 expression in adipose tissue or skeletal muscle promotes obesity. Lipin-2 and/or lipin-3 are capable of promoting VLDL synthesis and secretion
physiological function
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lipin-1 may be a mediator of glucocorticoid effects in conditions such as fasting and obesity, genetic variations in this response may contribute to interindividual variations in lipin-1 expression levels. Glucocorticoid-induced Lpin1 regulation leads to increased protein and PAP1 activity
physiological function
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lipin-1alpha may act as a sumoylation-regulated transcriptional coactivator in brain. Sumoylated forms of lipin-1 in muscle and liver are only marginally present. Lipin-1 (including both the alpha and beta isoforms) is modified by sumoylation at two consensus sumoylation sites, is sumoylated at relatively high levels in brain. No sumoylation of the related proteins lipin-2 and lipin-3
physiological function
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lipin-2 expression in adipose tissue may compensate for lack of lipin-1
physiological function
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lipin-2 has transcriptional coactivator activity for peroxisome proliferator-activated receptor-response elements similar to lipin-1. Lipin-1A activates PPRE-luciferase expression ca. 2fold
physiological function
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lipin1 reinforces the positive feedback loop between CCAAT/enhancer-binding protein alpha and peroxisome proliferator-activated receptor gamma2, which is essential for adipogenesis and the maintenance of adipocyte functions. Lipin1 is necessary and accelerates 3T3-L1 adipocyte differentiation. Lipin1 maintains the expression of adipocyte functional genes in 3T3-L1 mature adipocytes. Lipin1 functions by interacting with and activating peroxisome proliferator-activated receptor gamma2
physiological function
lpin-1 affects dynamics of the peripheral endoplasmic reticulum. The enzyme has no detectable effect on nuclear envelope assembly and expansion, but is crucially required for nuclear envelope breakdown and lamin depolymerization during mitosis. Lpin-1 acts independently of nuclear pore complexes and the transmembrane nucleoporin gp210
physiological function
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LPP1 forms both homo- and hetero-oligomers. Full catalytic activity is not required for oligomerization
physiological function
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LPP2 forms a complex with the 32 kDa form of LPP3, but not with the 34 kDa form. LPP oligomers may regulate compartmentalized pools of sphingosine 1-phosphate and phosphatidic acid and contribute to the spatial signalling by these lipids within cells
physiological function
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LPP3 contains arginine-glycine-glutamate (RGE) cell adhesion sequence, but murine LPP3 also interacts with alpha5beta1 and alphavalpha3 integrins. Transgenic mice that overexpress LPP1 demonstrate no significant differences in circulating lysophosphatidate concentrations compared with control mice. LPP3 functions as a Wnt signaling antagonist. Mice that overexpress LPP1 have decreased birth weight, sparse curly hair, and defective spermatogenesis causing infertility. LPP1 controls lysophosphatidate removal from the blood, which increases circulating lysophosphatidate levels. LPP2 regulates the timing of S-phase entry, but it is not essential for cell cycle progression
physiological function
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LPP3 contains arginine-glycine-glutamate (RGE) cell adhesion sequence. LPP2 activity regulates S-phase entry of the cell cycle in rat2 fibroblasts
physiological function
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LPP3 yields an 8fold increase in luciferase (lymphoid enhancer binding factor 1) activity
physiological function
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PAH1 and PAH2 are the phosphatidate phosphatase responsible for the eukaryotic pathway of galactolipid synthesis. Membrane lipid remodeling mediated by these two enzymes is an essential adaptation mechanism to cope with phosphate starvation. Complements yeast DELTAdpp1DELTAlpp1DELTApah1 in vivo
physiological function
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physiologically relevant increases in LPP1 activity in mouse embryonic fibroblasts (isolated from transgenic mice with 20 gene copies of LPP1) reduces lysophosphatidic acid- and platelet-derived growth factor-activation of ERK-1/2 and migration, resulting from down-regulation of typical proteinkinase C isoform(s) which are required for regulation of cell migration
physiological function
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stable overexpression of LPP1 or LPP2 reduces sphingosine 1-phosphate, lysophosphatidic acid- and thrombin-induced activation of ERK-1/2
physiological function
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sterol-mediated regulation of lipin 1 gene transcription modulates triglyceride accumulation
physiological function
the lipin1 gene may have a crucial effect on body lipid accumulation in pigs, whereas the lipin-beta isoform may play an important role in intramuscular fat deposition in obese pigs
physiological function
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wunen generates a phospholipid gradient and thereby repels germ cells towards higher phospholipid levels and away from the midline. Wunen/wunen-2 also governs the death of mis-migrating germ cells and survival of pole cells which compete for a common phospholipid substrate with somatic cells
physiological function
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forced expression of lipid phosphate phosphatase-3 in human colon tumor (SW-480) cells potentiates tumor growth via increased beta-catenin stability and cyclin-D1 synthesis. Elevated expression of lipid phosphate phosphatase-3 has no tumorigenic effects on primary cells. Lipid phosphate phosphatase-3 regulates glioblastoma cell migration
physiological function
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isoform lipin-1gamma plays a specialized role in regulating brain lipid metabolism
physiological function
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lipid phosphate phosphatase 2 is a part of abscisic acid signalling and participates to the regulation of stomatal movements
physiological function
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lipid phosphate phosphatase mediates germ cell-germ cell repulsion, this repulsion is necessary for germ cell dispersal and proper transepithelial migration at the onset of migration and for the equal sorting of the germ cells between the two embryonic gonads during their migration
physiological function
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lipin proteins play a dual function in lipid metabolism by acting as phosphatidate phosphatase enzymes and as transcriptional regulators. Lipin-1 is a key integrator of hormonal signals to the liver in diabetic dyslipidemia. Lipin-1 also induces the expression of key adipogenic transcription factors including PPARgamma and C/EBPalpha. Isoforms lipin-1alpha and lipin-1beta exert complementary roles in adipocyte differentiation. While lipin-1alpha induces the expression of adipogenic transcription factors, lipin-1beta induces the expression of lipid synthesis genes encoding, e.g., fatty acid synthase and diacylglycerol acyltransferase. Hepatic very low density lipoprotein synthesis and secretion is highly influenced by the expression of lipin-1. Membrane dynamics (conveyor) for very low density lipoprotein assembly/secretion are regulated by lipin-1
physiological function
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lipin proteins play a dual function in lipid metabolism by acting as phosphatidate phosphatase enzymes and as transcriptional regulators. Lipin-1 is a key integrator of hormonal signals to the liver in diabetic dyslipidemia. Lipin-1 also induces the expression of key adipogenic transcription factors including PPARgamma and C/EBPalpha. Isoforms lipin-1alpha and lipin-1beta exert complementary roles in adipocyte differentiation. While lipin-1alpha induces the expression of adipogenic transcription factors, lipin-1beta induces the expression of lipid synthesis genes encoding, e.g., fatty acid synthase and diacylglycerol acyltransferase. Hepatic very low density lipoprotein synthesis and secretion is highly influenced by the expression of lipin-1. Membrane dynamics (conveyor) for very low density lipoprotein assembly/secretion are regulated by lipin-1
physiological function
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lipin proteins play a dual function in lipid metabolism by acting as phosphatidate phosphatase enzymes and as transcriptional regulators. Lipin-1 is a key integrator of hormonal signals to the liver in diabetic dyslipidemia. Lipin-1 also induces the expression of key adipogenic transcription factors including PPARgamma and C/EBPalpha. Isoforms lipin-1alpha and lipin-1beta exert complementary roles in adipocyte differentiation. While lipin-1alpha induces the expression of adipogenic transcription factors, lipin-1beta induces the expression of lipid synthesis genes encoding, e.g., fatty acid synthase and diacylglycerol acyltransferase. Hepatic very low density lipoprotein synthesis and secretion is highly influenced by the expression of lipin-1. Membrane dynamics (conveyor) for very low density lipoprotein assembly/secretion are regulated by lipin-1
physiological function
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lipins are essential regulators of fat metabolism, adipogenesis, and organelle biogenesis
physiological function
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phosphatidate phosphatase activity is essential in protecting cells from palmitoleic acid (fatty acid)-induced toxicity
physiological function
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phosphatidic acid phosphatase enzymes, PAH1 and PAH2, are capable of repressing phospholipid biosynthesis at the endoplasmic reticulum in Arabidopsis thaliana. PAH1/2 play a role in the provision of eukaryotic substrate for galactolipid synthesis in leaves
physiological function
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the lipin 1 polybasic motif is critical for lipin1beta function in phospholipid and neutral lipid metabolism. Lipin1beta also functions as transcriptional coactivator. Both the transcriptional and metabolic functions of lipin 1 are required for full complementation of the adipogenic differentiation of lipin-deficient MEF cells. Lipin1 is also an amplifier of PGC-1alpha, a nuclear coactivator of PPAR-alpha responsive gene transcription
physiological function
conditional deletion of the enzyme gene leads to a decrease in the content of diacylglycerol and triacylglycerol, whereas its overexpression in both Rhodococcus jostii RHA1 and Rhodococcus opacus PD630 promotes an increase up to 10 to 15% by cellular dry weight in triacylglycerol content. Expression in the nonoleaginous strain Rhodococcus fascians F7 promotes an increase in total fatty acid content up to 7% at the expense of free fatty acid, diacylglycerol, and triacylglycerol fractions. Coexpression with Atf2 gene encoding wax ester/diacylglycerol acyltransferase results in a fourfold increase in total fatty acid content by a further increase of the free fatty acid and triacylglycerol fractions
physiological function
expression of the gene in yeast complements the temperature-sensitive growth phenotype of the phosphatidic acid phosphatase deficient strain GHY58. In Streptomyces coelicolor, disruption of either isoform lppalpha or lppbeta has no effect on triacylglycerol accumulation. The simultaneous mutation of both genes provokes a drastic reduction in de novo triacylglycerol biosynthesis as well as in total triacylglycerol content. Overexpression of Lppalpha and Lppbeta in the wild type strain of Streptomyces coelicolor leads to a significant increase in triacylglycerol production. Membrane proteins isolated from an Escherichia coli strain expressing Lppalpha and Lppbeta display a considerable increase in phosphatidic acid phosphatase activity compared with the control strain
physiological function
isoform Pah1p regulates lipid synthesis and composition throughout growth. An enzyme deletion mutant shows dramatic reductions in the synthesis of triacylglycerols and diacylglycerols and increases in synthesis of phospholipids, fatty acids, and ergosterol esters when compared with the wild type control. Pahip is dephosphorylated by the Nem1p-Spo7p protein phosphatase complex. Nem1 deletion mutant cells exhibit defects in triacylglycerol synthesis and lipid metabolism that mirror those imparted by the Pah1 deletion mutation
physiological function
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isoform PAH2 possesses the minimal function of phosphatidate phosphatase protein family in respiration. The enzyme is not essential for the normal growth and survival of Tetrahymena
physiological function
lipid phosphate phosphatase 3 regulates adipocyte sphingolipid synthesis, but not developmental adipogenesis or diet-induced obesity in mice
physiological function
LPP3 activity is crucial for vascular and heart development
physiological function
LPP3 activity is crucial for vascular and heart development
physiological function
LPP3 is a negative regulator of inflammatory cytokines, leucocyte adhesion, cell survival, and migration in human primary aortic endothelial cells, suggesting a protective role of LPP3 against endothelial dysfunction in humans
physiological function
LPP3 regulates intracellular and extracellular lysophosphatidic acid and sphingosine-1-phosphate signalling through the dephosphorylation of these bioactive lipids
physiological function
LPP3 regulates intracellular and extracellular lysophosphatidic acid and sphingosine-1-phosphate signalling through the dephosphorylation of these bioactive lipids
physiological function
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the enzyme activity is required to support hepatitis C virus infection
physiological function
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the enzyme plays an important role in hyphal growth, adaptability to environmental stresses, and virulence
physiological function
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isoform PAH2 possesses the minimal function of phosphatidate phosphatase protein family in respiration. The enzyme is not essential for the normal growth and survival of Tetrahymena
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physiological function
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lipin-2 has transcriptional coactivator activity for peroxisome proliferator-activated receptor-response elements similar to lipin-1. Lipin-1A activates PPRE-luciferase expression ca. 2fold
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physiological function
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expression of the gene in yeast complements the temperature-sensitive growth phenotype of the phosphatidic acid phosphatase deficient strain GHY58. In Streptomyces coelicolor, disruption of either isoform lppalpha or lppbeta has no effect on triacylglycerol accumulation. The simultaneous mutation of both genes provokes a drastic reduction in de novo triacylglycerol biosynthesis as well as in total triacylglycerol content. Overexpression of Lppalpha and Lppbeta in the wild type strain of Streptomyces coelicolor leads to a significant increase in triacylglycerol production. Membrane proteins isolated from an Escherichia coli strain expressing Lppalpha and Lppbeta display a considerable increase in phosphatidic acid phosphatase activity compared with the control strain
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physiological function
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isoform PAH2 possesses the minimal function of phosphatidate phosphatase protein family in respiration. The enzyme is not essential for the normal growth and survival of Tetrahymena
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physiological function
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phosphatidate phosphatase activity is essential in protecting cells from palmitoleic acid (fatty acid)-induced toxicity
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