Difference between revisions of "YMR165C"
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| − | '''Description of YMR165C:''' | + | '''Description of YMR165C:''' Mg2+-dependent phosphatidate (PA) phosphatase; catalyzes dephosphorylation of PA to yield diacylglycerol; responsible for de novo lipid synthesis and formation of lipid droplets; phosphorylation by Pho80p-Pho85p decreases catalytic activity and alters Pah1p localization and abundance; phosphorylation by protein kinase A decreases catalytic efficiency; dephosphorylation by Nem1p-Spo7p anchors Pah1p to the membrane increasing substrate catalysis; homologous to mammalian lipin 1<ref name='S000144790'>Adeyo O, et al. (2011) The yeast lipin orthologue Pah1p is important for biogenesis of lipid droplets. J Cell Biol 192(6):1043-55 {{SGDpaper|S000144790}} PMID 21422231</ref><ref name='S000148373'>Choi HS, et al. (2012) Pho85p-Pho80p phosphorylation of yeast Pah1p phosphatidate phosphatase regulates its activity, location, abundance, and function in lipid metabolism. J Biol Chem () {{SGDpaper|S000148373}} PMID 22334681</ref><ref name='S000114345'>Han GS, et al. (2006) The Saccharomyces cerevisiae Lipin homolog is a Mg2+-dependent phosphatidate phosphatase enzyme. J Biol Chem 281(14):9210-8 {{SGDpaper|S000114345}} PMID 16467296</ref><ref name='S000150466'>Su WM, et al. (2012) Protein Kinase A-mediated Phosphorylation of Pah1p Phosphatidate Phosphatase Functions in Conjunction with the Pho85p-Pho80p and Cdc28p-Cyclin B Kinases to Regulate Lipid Synthesis in Yeast. J Biol Chem () |
| − | {{SGDpaper| | + | {{SGDpaper|S000150466}} PMID 22865862</ref> |
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Revision as of 13:05, 6 September 2012
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| Systematic name | YMR165C |
| Gene name | PAH1 |
| Aliases | SMP2 |
| Feature type | ORF, Verified |
| Coordinates | Chr XIII:592628..590040 |
| Primary SGDID | S000004775 |
Description of YMR165C: Mg2+-dependent phosphatidate (PA) phosphatase; catalyzes dephosphorylation of PA to yield diacylglycerol; responsible for de novo lipid synthesis and formation of lipid droplets; phosphorylation by Pho80p-Pho85p decreases catalytic activity and alters Pah1p localization and abundance; phosphorylation by protein kinase A decreases catalytic efficiency; dephosphorylation by Nem1p-Spo7p anchors Pah1p to the membrane increasing substrate catalysis; homologous to mammalian lipin 1[1][2][3][4]
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References
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- ↑ Adeyo O, et al. (2011) The yeast lipin orthologue Pah1p is important for biogenesis of lipid droplets. J Cell Biol 192(6):1043-55 SGD PMID 21422231
- ↑ Choi HS, et al. (2012) Pho85p-Pho80p phosphorylation of yeast Pah1p phosphatidate phosphatase regulates its activity, location, abundance, and function in lipid metabolism. J Biol Chem () SGD PMID 22334681
- ↑ Han GS, et al. (2006) The Saccharomyces cerevisiae Lipin homolog is a Mg2+-dependent phosphatidate phosphatase enzyme. J Biol Chem 281(14):9210-8 SGD PMID 16467296
- ↑ Su WM, et al. (2012) Protein Kinase A-mediated Phosphorylation of Pah1p Phosphatidate Phosphatase Functions in Conjunction with the Pho85p-Pho80p and Cdc28p-Cyclin B Kinases to Regulate Lipid Synthesis in Yeast. J Biol Chem () SGD PMID 22865862
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