ArticleThe Journal of biological chemistry2012
Pho85p-Pho80p phosphorylation of yeast Pah1p phosphatidate phosphatase regulates its activity, location, abundance, and function in lipid metabolism.
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 69 papers.
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Who cites it
69 citing papers in PubMed, 101 citations in OpenAlex.
- Crosstalk between protein kinases Pho85-Pho80 and Rim11 regulates Pah1 phosphatidate phosphatase function in lipid synthesis.The Journal of biological chemistry · 2026Article
- Multi-omics reveal phosphatidic acid phosphatases modify Niemann-Pick type C disease severity.iScience · 2026Article
- 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
- Uncovering the Role of the Yeast Lysine Acetyltransferase NuA4 in the Regulation of Nuclear Shape and Lipid Metabolism.Molecular and cellular 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
- LPIN2 is the phosphatase dominating the penultimate step of neutral lipid biosynthesis inmicroPublication biology · 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
- The Phosphatase Cascade Nem1/Spo7-Pah1 Regulates Fungal Development, Lipid Homeostasis, and Virulence in Botryosphaeria dothidea.Microbiology spectrum · 2023Article
- A Yeast Mitotic Tale for the Nucleus and the Vacuoles to Embrace.International journal of molecular sciences · 2023Review
- Phosphorylation-mediated regulation of the Nem1-Spo7/Pah1 phosphatase cascade in yeast lipid synthesis.Advances in biological regulation · 2022Review
- TheFrontiers in microbiology · 2022Article
- 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 of Nutrient Signaling Pathways Conserved in Arbuscular Mycorrhizal Fungi.Microorganisms · 2021Article
- A review of phosphatidate phosphatase assays.Journal of lipid research · 2020Review
- 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
- Crystal structure of a lipin/Pah phosphatidic acid phosphatase.Nature communications · 2020Article
- Pho85 and PI(4,5)PBiochimica et biophysica acta. Molecular and cell biology of lipids · 2020Article
9 more citing papers are in PubMed but not listed here.
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6 authors at 1 institution in 1 country.
Funding
Abstract
The yeast Pah1p phosphatidate phosphatase, which catalyzes the penultimate step in the synthesis of triacylglycerol and plays a role in the transcriptional regulation of phospholipid synthesis genes, is a cytosolic enzyme that associates with the nuclear/endoplasmic reticulum membrane to catalyze the dephosphorylation of phosphatidate to yield diacylglycerol. Pah1p is phosphorylated on seven (Ser-110, Ser-114, Ser-168, Ser-602, Thr-723, Ser-744, and Ser-748) sites that are targets for proline-directed protein kinases. In this work, we showed that the seven sites are phosphorylated by Pho85p-Pho80p, a protein kinase-cyclin complex known to regulate a variety of cellular processes. The phosphorylation of recombinant Pah1p was time- and dose-dependent and dependent on the concentrations of ATP (3.7 μm) and Pah1p (0.25 μm). Phosphorylation reduced (6-fold) the catalytic efficiency (V(max)/K(m)) of Pah1p and reduced (3-fold) its interaction (K(d)) with liposomes. Alanine mutations of the seven sites ablated the inhibitory effect that Pho85p-Pho80p had on Pah1p activity and on the interaction with liposomes. Analysis of pho85Δ mutant cells, phosphate-starved wild type cells, and cells expressing phosphorylation-deficient forms of Pah1p indicated that loss of Pho85p-Pho80p phosphorylation reduced Pah1p abundance. In contrast, lack of Nem1p-Spo7p, the phosphatase complex that dephosphorylates Pah1p at the nuclear/endoplasmic reticulum membrane, stabilized Pah1p abundance. Although loss of phosphorylation caused a decrease in abundance, a greater amount of Pah1p was associated with membranes when compared with phosphorylated enzyme, and the loss of phosphorylation allowed bypass of the Nem1p-Spo7p requirement for Pah1p function in the synthesis of triacylglycerol.
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