Pho85p-Pho80p phosphorylation of yeast Pah1p phosphatidate phosphatase regulates its activity, location, abundance, and function in lipid metabolism.

The Journal of Biological Chemistry
Hyeon-Son ChoiGeorge M Carman

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 Pah...Continue Reading

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Citations

Dec 26, 2012·Proceedings of the National Academy of Sciences of the United States of America·Mayurranjan S MitraBrian N Finck
Oct 17, 2012·The Journal of Biological Chemistry·Minjung ChaeGeorge M Carman
Mar 1, 2013·Molecular Biology of the Cell·Marisa Kirchenbauer, Dimitris Liakopoulos
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