ArticleThe Journal of biological chemistry2014
Yeast Nem1-Spo7 protein phosphatase activity on Pah1 phosphatidate phosphatase is specific for the Pho85-Pho80 protein kinase phosphorylation sites.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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39 citing papers in PubMed, 61 citations in OpenAlex.
- Lipid remodeling enables adaptation to chronic hyperosmotic stress.The Journal of cell biology · 2026Article
- Crosstalk between protein kinases Pho85-Pho80 and Rim11 regulates Pah1 phosphatidate phosphatase function in lipid synthesis.The Journal of biological chemistry · 2026Article
- Seipin-defined ER sites undergo distinct enrichment of factors for the biogenesis of sterol ester rich lipid droplets.iScience · 2026Article
- Pex30-dependent membrane contact sites maintain ER lipid homeostasis.The Journal of cell biology · 2025Article
- Insights into phosphatidic acid phosphatase and its potential role as a therapeutic target.Advances in biological regulation · 2025Review
- Architecture and function of yeast phosphatidate phosphatase Pah1 domains/regions.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2024Review
- p53 ensures the normal behavior and modification of G1/S-specific histone H3.1 in the nucleus.Life science alliance · 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
- Valproate regulates inositol synthesis by reducing expression of myo-inositol-3-phosphate synthase.Scientific reports · 2023Article
- SUMOylation at the inner nuclear membrane facilitates nuclear envelope biogenesis during mitosis.The Journal of cell biology · 2023Article
- Phosphorylation-mediated regulation of the Nem1-Spo7/Pah1 phosphatase cascade in yeast lipid synthesis.Advances in biological regulation · 2022Review
- Recent progress in strategies for steroid production in yeasts.World journal of microbiology & biotechnology · 2022Review
- Reengineering of 7-dehydrocholesterol biosynthesis inFrontiers in microbiology · 2022Article
- Ice2 promotes ER membrane biogenesis in yeast by inhibiting the conserved lipin phosphatase complex.The EMBO journal · 2021Article
- NLIP and HAD-like Domains of Pah1 and Lipin 1 Phosphatidate Phosphatases Are Essential for Their Catalytic Activities.Molecules (Basel, Switzerland) · 2021Article
- Torsin and NEP1R1-CTDNEP1 phosphatase affect interphase nuclear pore complex insertion by lipid-dependent and lipid-independent mechanisms.The EMBO journal · 2021Article
- The Spo7 sequence LLI is required for Nem1-Spo7/Pah1 phosphatase cascade function in yeast lipid metabolism.The Journal of biological chemistry · 2020Article
- Yeast phosphatidic acid phosphatase Pah1 hops and scoots along the membrane phospholipid bilayer.Journal of lipid research · 2020Article
- Pho85 and PI(4,5)PBiochimica et biophysica acta. Molecular and cell biology of lipids · 2020Article
- Phosphatidate-mediated regulation of lipid synthesis at the nuclear/endoplasmic reticulum membrane.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2020Review
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3 authors at 1 institution in 1 country.
Funding
Abstract
Pah1 is the phosphatidate phosphatase in the yeast Saccharomyces cerevisiae that produces diacylglycerol for triacylglycerol synthesis and concurrently controls the levels of phosphatidate used for phospholipid synthesis. Phosphorylation and dephosphorylation of Pah1 regulate its subcellular location and phosphatidate phosphatase activity. Compared with its phosphorylation by multiple protein kinases, Pah1 is dephosphorylated by a protein phosphatase complex consisting of Nem1 (catalytic subunit) and Spo7 (regulatory subunit). In this work, we characterized the Nem1-Spo7 phosphatase complex for its enzymological, kinetic, and regulatory properties with phosphorylated Pah1. The dephosphorylation of Pah1 by Nem1-Spo7 phosphatase resulted in the stimulation (6-fold) of phosphatidate phosphatase activity. For Pah1 phosphorylated by the Pho85-Pho80 kinase complex, maximum Nem1-Spo7 phosphatase activity required Mg(2+) ions (8 mm) and Triton X-100 (0.25 mm) at pH 5.0. The energy of activation for the reaction was 8.4 kcal/mol, and the enzyme was thermally labile at temperatures above 40 °C. The enzyme activity was inhibited by sodium vanadate, sodium fluoride, N-ethylmaleimide, and phenylglyoxal but was not significantly affected by lipids or nucleotides. Nem1-Spo7 phosphatase activity was dependent on the concentrations of Pah1 phosphorylated by Pho85-Pho80, Cdc28-cyclin B, PKA, and PKC with kcat and Km values of 0.29 s(-1) and 81 nm, 0.11 s(-1) and 127 nm, 0.10 s(-1) and 46 nm, and 0.02 s(-1) and 38 nm, respectively. Its specificity constant (kcat/Km) for Pah1 phosphorylated by Pho85-Pho80 was 1.6-, 4-, and 6-fold higher, respectively, than that phosphorylated by PKA, Cdc28-cyclin B, and PKC.
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