increases the phosphorylation of multiple sites, markedly increases the amounts of lipin and PAP activity in the soluble fraction, effects of insulin are attenuated by rapamycin or by inhibiting PI 3 kinase
essential for optimal activity, responsible for a better solubilization of the substrate by CHAPS. The possibility of a specidic role as aphysiological activator cannot be ruled out
increases hydrolysis of phosphatidate bound to microsomal membrane or phosphatidate in sonicated dispersion of organic solvent-disrupted microsomes, little effect on hydrolysis of phosphatidate dispersed in sonicated microsomal lipid
treatment of HeLa cells with the epidermal growth factor leads to 3fold increased LPP-3 expression, while LPP-1 expression is unaffected, LPP-1 expression is increased in prostate adenocarcinoma cells treated with androgens
treatment of HeLa cells with the epidermal growth factor leads to 3fold increased LPP-3 expression, while LPP-1 expression is unaffected, LPP-1 expression is increased in prostate adenocarcinoma cells treated with androgens
treatment of HeLa cells with the epidermal growth factor leads to 3fold increased LPP-3 expression, while LPP-1 expression is unaffected, LPP-1 expression is increased in prostate adenocarcinoma cells treated with androgens
treatment of HeLa cells with the epidermal growth factor leads to 3fold increased LPP-3 expression, while LPP-1 expression is unaffected, LPP-1 expression is increased in prostate adenocarcinoma cells treated with androgens
insulin increases the phosphorylation of multiple sites e.g. at Ser106, insulin and epinephrine control lipin primarily by changing localization rather than intrinsic PAP activity, overview
hepatic lipin 2 protein content is markedly increased by lipin 1 deficiency, food deprivation, and obesity, often independent of changes in steady-state mRNA levels. Fasting induces expression of Lpin1 and Lpin2 in wild-type and PGC-1alpha-deficient mice
hyperactivated TORC2 enhances expression of lipin1. Diet-induced or genetic obesity increases LIPIN1 expression in mouse liver, and TORC2 is responsible for its transcriptional activation
increasing the catalytic activity of LPP1 decreases the pertussis toxin-sensitive stimulation of fibroblast migration by lyso-phosphatidic acid and an lyso-phosphatidic acid-receptor agonist, that can not be dephosphorylated
expression of the DPP1 gene, which encodes DGPP phosphatase, is induced by zinc depletion, by inositol supplementation, and when cells enter the stationary phase, induction by zinc depletion is mediated by the transcription factor Zap1p, which binds to a zinc-responsive element in the DPP1 promoter
the transcription factor Zap1p binds the DPP1 promoter and induces the expression of DGPP phosphatase, stress condition of zinc depletion induces DPP1 expression
dephosphorylation of lipin Pah1p by the Nem1p-Spo7p complex enables the amphipathic helix to anchor Pah1p onto the nuclear/endoplasmic reticulum membrane allowing the production of diacylglycerol for lipid biosynthesis
the enzyme expression is drought-stimulated. Transcripts accumulate in response to water deficit, including progressive dehydration of whole plants and rapid desiccation of detached leaves. The isozymes are not affected by wounding or by treatment with jasmonic acid