Difference between revisions of "YMR165C"
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| − | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http:// | + | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000004775 YMR165C] |
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''PAH1 '' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''PAH1 '' | ||
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| − | '''Description of YMR165C:''' | + | '''Description of YMR165C:''' Mg2+-dependent phosphatidate (PA) phosphatase; dephosphorylates 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 lipins 1 and 2<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='S000151210'>Grimsey N, et al. (2008) Temporal and spatial regulation of the phosphatidate phosphatases lipin 1 and 2. J Biol Chem 283(43):29166-74 {{SGDpaper|S000151210}} PMID 18694939</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='S000137195'>Karanasios E, et al. (2010) A phosphorylation-regulated amphipathic helix controls the membrane translocation and function of the yeast phosphatidate phosphatase. Proc Natl Acad Sci U S A 107(41):17539-44 {{SGDpaper|S000137195}} PMID 20876142</ref><ref name='S000081991'>Santos-Rosa H, et al. (2005) The yeast lipin Smp2 couples phospholipid biosynthesis to nuclear membrane growth. EMBO J 24(11):1931-41 {{SGDpaper|S000081991}} PMID 15889145</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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Latest revision as of 14:05, 4 October 2012
Share your knowledge...Edit this entry! <protect>
| 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; dephosphorylates 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 lipins 1 and 2[1][2][3][4][5][6][7]
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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
- ↑ Grimsey N, et al. (2008) Temporal and spatial regulation of the phosphatidate phosphatases lipin 1 and 2. J Biol Chem 283(43):29166-74 SGD PMID 18694939
- ↑ 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
- ↑ Karanasios E, et al. (2010) A phosphorylation-regulated amphipathic helix controls the membrane translocation and function of the yeast phosphatidate phosphatase. Proc Natl Acad Sci U S A 107(41):17539-44 SGD PMID 20876142
- ↑ Santos-Rosa H, et al. (2005) The yeast lipin Smp2 couples phospholipid biosynthesis to nuclear membrane growth. EMBO J 24(11):1931-41 SGD PMID 15889145
- ↑ 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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