Difference between revisions of "YMR165C"

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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?locus=YMR165C YMR165C]  
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|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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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
 
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|nowrap| Chr XIII:592627..590039
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|nowrap| Chr XIII:592628..590040
 
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''          || S000004775
 
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'''Description of {{PAGENAME}}:''' Mg<sup>2+</sup>-dependent phosphatidate (PA) phosphatase, catalyzes the dephosphorylation of PA to yield diacylglycerol and P<sub>i</sub>, responsible for de novo lipid synthesis; homologous to mammalian lipin 1<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
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'''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 ()
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  {{SGDpaper|S000150466}} PMID 22865862</ref>
 
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==Community Commentary==
 
==Community Commentary==
 
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Specifically higher expression in carbon limited chemostat cultures versus carbon excess.
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<ref>Boer VM, et al. (2003) The genome-wide transcriptional responses of Saccharomyces cerevisiae grown on glucose in aerobic chemostat cultures limited for carbon, nitrogen, phosphorus, or sulfur.
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J Biol Chem 278(5):3265-74</ref>
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==References==
 
==References==
 
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Latest revision as of 13:05, 4 October 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; 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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  1. ↑ 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
  2. ↑ 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
  3. ↑ 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
  4. ↑ 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
  5. ↑ 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
  6. ↑ 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
  7. ↑ 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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