Phosphorylation of Yeast Pah1 Phosphatidate Phosphatase by Casein Kinase II Regulates Its Function in Lipid Metabolism

• Published in: The Journal of biological chemistry Vol. 291; no. 19; pp. 9974 - 9990
• Main Authors: Hsieh, Lu-Sheng, Su, Wen-Min, Han, Gil-Soo, Carman, George M.
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 06.05.2016; American Society for Biochemistry and Molecular Biology
• Subjects: Amino Acid Substitution; Casein Kinase II - genetics; Casein Kinase II - metabolism; diacylglycerol; lipid; Lipids; Mass Spectrometry; Mutagenesis, Site-Directed; Mutation, Missense; phosphatidate; Phosphatidate Phosphatase - genetics; Phosphatidate Phosphatase - metabolism; phospholipid; phosphorylation; Phosphorylation - physiology; Saccharomyces cerevisiae - enzymology; Saccharomyces cerevisiae - genetics; Saccharomyces cerevisiae Proteins - genetics; Saccharomyces cerevisiae Proteins - metabolism; triacylglycerol; Triglycerides - genetics; Triglycerides - metabolism; yeast; triacylglycerol; phosphatidate; phospholipid; lipid; phosphorylation; diacylglycerol; yeast

Pah1 phosphatidate phosphatase in Saccharomyces cerevisiae catalyzes the penultimate step in the synthesis of triacylglycerol (i.e. the production of diacylglycerol by dephosphorylation of phosphatidate). The enzyme playing a major role in lipid metabolism is subject to phosphorylation (e.g. by Pho8...