ArticleMolecular biology of the cell2013
Regulation of lipid droplet and membrane biogenesis by the acidic tail of the phosphatidate phosphatase Pah1p.
Article in Molecular biology of the cell, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.
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Who cites it
62 citing papers in PubMed, 100 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
- A CRISPR-Cas9-based system for the dose-dependent study of DNA double-strand break sensing and repair.The FEBS journal · 2025Article
- UBE2J2 sensitizes the ERAD ubiquitination cascade to changes in membrane lipid saturation.Nature communications · 2025Article
- Phosphatidic acid drives spatiotemporal distribution of Pex30 at ER-LD contact sites.The Journal of cell biology · 2025Article
- Insights into phosphatidic acid phosphatase and its potential role as a therapeutic target.Advances in biological regulation · 2025Review
- Seipin governs phosphatidic acid homeostasis at the inner nuclear membrane.Nature communications · 2024Article
- Architecture and function of yeast phosphatidate phosphatase Pah1 domains/regions.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2024Review
- Differential reliance of CTD-nuclear envelope phosphatase 1 on its regulatory subunit in ER lipid synthesis and storage.Molecular biology of the cell · 2024Article
- Structure and mechanism of the human CTDNEP1-NEP1R1 membrane protein phosphatase complex necessary to maintain ER membrane morphology.Proceedings of the National Academy of Sciences of the United States of America · 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
- Uncovering the Role of the Yeast Lysine Acetyltransferase NuA4 in the Regulation of Nuclear Shape and Lipid Metabolism.Molecular and cellular biology · 2024Article
- Concept of lipid droplet biogenesis.European journal of cell biology · 2023Review
- A sterol-PI(4)P exchanger modulates the Tel1/ATM axis of the DNA damage response.The EMBO journal · 2023Article
- The Phosphatase Cascade Nem1/Spo7-Pah1 Regulates Fungal Development, Lipid Homeostasis, and Virulence in Botryosphaeria dothidea.Microbiology spectrum · 2023Article
- A lipid droplet-associated protein Nem1 regulates appressorium function for infection ofaBIOTECH · 2023Article
- Compartmentalization engineering of yeasts to overcome precursor limitations and cytotoxicity in terpenoid production.Frontiers in bioengineering and biotechnology · 2023Review
- Nuclear ingression of cytoplasmic bodies accompanies a boost in autophagy.Life science alliance · 2022Article
- Phosphorylation-mediated regulation of the Nem1-Spo7/Pah1 phosphatase cascade in yeast lipid synthesis.Advances in biological regulation · 2022Review
- 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
2 more citing papers are in PubMed but not listed here.
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Authors and funding
8 authors at 3 institutions in 3 countries.
Funding
Abstract
Lipins are evolutionarily conserved phosphatidate phosphatases that perform key functions in phospholipid, triglyceride, and membrane biogenesis. Translocation of lipins on membranes requires their dephosphorylation by the Nem1p-Spo7p transmembrane phosphatase complex through a poorly understood mechanism. Here we identify the carboxy-terminal acidic tail of the yeast lipin Pah1p as an important regulator of this step. Deletion or mutations of the tail disrupt binding of Pah1p to the Nem1p-Spo7p complex and Pah1p membrane translocation. Overexpression of Nem1p-Spo7p drives the recruitment of Pah1p in the vicinity of lipid droplets in an acidic tail-dependent manner and induces lipid droplet biogenesis. Genetic analysis shows that the acidic tail is essential for the Nem1p-Spo7p-dependent activation of Pah1p but not for the function of Pah1p itself once it is dephosphorylated. Loss of the tail disrupts nuclear structure, INO1 gene expression, and triglyceride synthesis. Similar acidic sequences are present in the carboxy-terminal ends of all yeast lipin orthologues. We propose that acidic tail-dependent binding and dephosphorylation of Pah1p by the Nem1p-Spo7p complex is an important determinant of its function in lipid and membrane biogenesis.
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