Phosphatidate phosphatase Pah1 contains a novel RP domain that regulates its phosphorylation and function in yeast lipid synthesis
Author:
Funder
U.S. Public Health Service
National Institutes of Health
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference105 articles.
1. Fat-regulating phosphatidic acid phosphatase: a review of its roles and regulation in lipid homeostasis;Carman;J. Lipid Res.,2019
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3. Phosphatidic acid phosphatase, a key enzyme in the regulation of lipid synthesis;Carman;J. Biol. Chem.,2009
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5. The Saccharomyces cerevisiae lipin homolog is a Mg2+-dependent phosphatidate phosphatase enzyme;Han;J. Biol. Chem.,2006
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1. Architecture and function of yeast phosphatidate phosphatase Pah1 domains/regions;Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids;2024-12
2. Protein kinase Hsl1 phosphorylates Pah1 to inhibit phosphatidate phosphatase activity and regulate lipid synthesis in Saccharomyces cerevisiae;Journal of Biological Chemistry;2024-08
3. Therapeutic potential of lipin inhibitors for the treatment of cancer;Biochemical Pharmacology;2024-04
4. Catalytic core function of yeast Pah1 phosphatidate phosphatase reveals structural insight into its membrane localization and activity control;Journal of Biological Chemistry;2024-01
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