ArticleThe Journal of biological chemistry2012
The Saccharomyces cerevisiae actin patch protein App1p is a phosphatidate phosphatase enzyme.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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38 citing papers in PubMed, 65 citations in OpenAlex.
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- Engineering yeast for tailored fatty acid profiles.Applied microbiology and biotechnology · 2025Review
- A genome-wide CRISPR screen identifies GRA38 as a key regulator of lipid homeostasis duringResearch square · 2025Article
- Insights into phosphatidic acid phosphatase and its potential role as a therapeutic target.Advances in biological regulation · 2025Review
- The PAH1-encoded phosphatidate phosphatase of Yarrowia lipolytica differentially affects gene expression and lipid biosynthesis.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2024Article
- Architecture and function of yeast phosphatidate phosphatase Pah1 domains/regions.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2024Review
- Manipulating multi-level selection in a fungal entomopathogen reveals social conflicts and a method for improving biocontrol traits.PLoS pathogens · 2024Article
- LPIN2 is the phosphatase dominating the penultimate step of neutral lipid biosynthesis inmicroPublication biology · 2024Article
- The Saccharomyces cerevisiae Spo7 basic tail is required for Nem1-Spo7/Pah1 phosphatase cascade function in lipid synthesis.The Journal of biological chemistry · 2024Article
- The Lipid Profile of theJournal of fungi (Basel, Switzerland) · 2022Article
- Leishmania guyanensis M4147 as a new LRV1-bearing model parasite: Phosphatidate phosphatase 2-like protein controls cell cycle progression and intracellular lipid content.PLoS neglected tropical diseases · 2022Article
- Phosphorylation-mediated regulation of the Nem1-Spo7/Pah1 phosphatase cascade in yeast lipid synthesis.Advances in biological regulation · 2022Review
- NLIP and HAD-like Domains of Pah1 and Lipin 1 Phosphatidate Phosphatases Are Essential for Their Catalytic Activities.Molecules (Basel, Switzerland) · 2021Article
- Genome-wide analysis and expression patterns of lipid phospholipid phospholipase gene family in Brassica napus L.BMC genomics · 2021Article
- Toxoplasma LIPIN is essential in channeling host lipid fluxes through membrane biogenesis and lipid storage.Nature communications · 2021Article
- Improved production of germacrene A, a direct precursor of ß-elemene, in engineered Saccharomyces cerevisiae by expressing a cyanobacterial germacrene A synthase.Microbial cell factories · 2021Article
- A review of phosphatidate phosphatase assays.Journal of lipid research · 2020Review
- Phosphatidate-mediated regulation of lipid synthesis at the nuclear/endoplasmic reticulum membrane.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2020Review
- Discoveries of the phosphatidate phosphatase genes in yeast published in theThe Journal of biological chemistry · 2019Review
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3 authors at 1 institution in 1 country.
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Abstract
backgroundPhosphatidate phosphatase (PAP) plays diverse roles in lipid metabolism and cell signaling.
resultsA novel yeast PAP is identified as the actin patch protein encoded by APP1.
conclusionAPP1 and other known genes (PAH1, DPP1, LPP1) are responsible for all detectable PAP activity in yeast. SIGNIFICANCE: Identification of App1p as a PAP enzyme will facilitate the understanding of its cellular function. Phosphatidate phosphatase (PAP) catalyzes the dephosphorylation of phosphatidate to yield diacylglycerol. In the yeast Saccharomyces cerevisiae, PAP is encoded by PAH1, DPP1, and LPP1. The presence of PAP activity in the pah1Δ dpp1Δ lpp1Δ triple mutant indicated another gene(s) encoding the enzyme. We purified PAP from the pah1Δ dpp1Δ lpp1Δ triple mutant by salt extraction of mitochondria followed by chromatography with DE52, Affi-Gel Blue, phenyl-Sepharose, MonoQ, and Superdex 200. Liquid chromatography/tandem mass spectrometry analysis of a PAP-enriched sample revealed multiple putative phosphatases. By analysis of PAP activity in mutants lacking each of the proteins, we found that APP1, a gene whose molecular function has been unknown, confers ~30% PAP activity of wild type cells. The overexpression of APP1 in the pah1Δ dpp1Δ lpp1Δ mutant exhibited a 10-fold increase in PAP activity. The PAP activity shown by App1p heterologously expressed in Escherichia coli confirmed that APP1 is the structural gene for the enzyme. Introduction of the app1Δ mutation into the pah1Δ dpp1Δ lpp1Δ triple mutant resulted in a complete loss of PAP activity, indicating that distinct PAP enzymes in S. cerevisiae are encoded by APP1, PAH1, DPP1, and LPP1. Lipid analysis of cells lacking the PAP genes, singly or in combination, showed that Pah1p is the only PAP involved in the synthesis of triacylglycerol as well as in the regulation of phospholipid synthesis. App1p, which shows interactions with endocytic proteins, may play a role in vesicular trafficking through its PAP activity.
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