Difference between revisions of "YKR089C"

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'''Description of YKR089C:''' Triacylglycerol lipase involved in triacylglycerol mobilization and degradation; found in lipid particles; phosphorylated and activated by Cdc28p; required with Tgl3p for timely bud formation<ref name='S000087074'>Kurat CF, et al. (2006) Obese yeast: triglyceride lipolysis is functionally conserved from mammals to yeast. J Biol Chem 281(1):491-500 {{SGDpaper|S000087074}} PMID 16267052</ref><ref name='S000086466'>Athenstaedt K and Daum G (2005) Tgl4p and Tgl5p, two triacylglycerol lipases of the yeast Saccharomyces cerevisiae are localized to lipid particles. J Biol Chem 280(45):37301-9 {{SGDpaper|S000086466}} PMID 16135509</ref><ref name='S000074306'>Ubersax JA, et al. (2003) Targets of the cyclin-dependent kinase Cdk1. Nature 425(6960):859-64 {{SGDpaper|S000074306}} PMID 14574415</ref><ref name='S000129072'>Kurat CF, et al. (2009) Cdk1/Cdc28-dependent activation of the major triacylglycerol lipase Tgl4 in yeast links lipolysis to cell-cycle progression. Mol Cell 33(1):53-63
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'''Description of YKR089C:''' Triacylglycerol lipase involved in triacylglycerol mobilization and degradation; found in lipid particles; phosphorylated and activated by Cdc28p; required with Tgl3p for timely bud formation<ref name='S000086466'>Athenstaedt K and Daum G (2005) Tgl4p and Tgl5p, two triacylglycerol lipases of the yeast Saccharomyces cerevisiae are localized to lipid particles. J Biol Chem 280(45):37301-9 {{SGDpaper|S000086466}} PMID 16135509</ref><ref name='S000087074'>Kurat CF, et al. (2006) Obese yeast: triglyceride lipolysis is functionally conserved from mammals to yeast. J Biol Chem 281(1):491-500 {{SGDpaper|S000087074}} PMID 16267052</ref><ref name='S000129072'>Kurat CF, et al. (2009) Cdk1/Cdc28-dependent activation of the major triacylglycerol lipase Tgl4 in yeast links lipolysis to cell-cycle progression. Mol Cell 33(1):53-63 {{SGDpaper|S000129072}} PMID 19150427</ref><ref name='S000074306'>Ubersax JA, et al. (2003) Targets of the cyclin-dependent kinase Cdk1. Nature 425(6960):859-64
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Revision as of 13:05, 25 February 2010

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Systematic name YKR089C
Gene name TGL4
Aliases STC1
Feature type ORF, Verified
Coordinates Chr XI:608007..605275
Primary SGDID S000001797


Description of YKR089C: Triacylglycerol lipase involved in triacylglycerol mobilization and degradation; found in lipid particles; phosphorylated and activated by Cdc28p; required with Tgl3p for timely bud formation[1][2][3][4]




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Community Commentary

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Alleles, Strains, and Phenotypes

Multiple Knockout Strains

Together with: TGL3
Phenotype(s): Loss of function (Null), Recessive, Viable

tgl3 tgl4 double mutants are unable to degrade triglycerides in lag and early log-phases of growth [2] [5]

Protein Details

Protein Function/Process

Together with: TGL3

Triglyceride lipase activity; Functional complementation of tgl4 mutants by murine ATGL, Adipose Triglyceride Lipase [2] [5]

Protein Modification

Modification(s): Phosphorylation

Identified as an efficient substrate of Clb2-Cdk1-as1 in a screen of a proteomic GST-fusion library. [4] [6]




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References

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  1. ↑ Athenstaedt K and Daum G (2005) Tgl4p and Tgl5p, two triacylglycerol lipases of the yeast Saccharomyces cerevisiae are localized to lipid particles. J Biol Chem 280(45):37301-9 SGD PMID 16135509
  2. ↑ 2.0 2.1 2.2 Kurat CF, et al. (2006) Obese yeast: triglyceride lipolysis is functionally conserved from mammals to yeast. J Biol Chem 281(1):491-500 SGD PMID 16267052
  3. ↑ Kurat CF, et al. (2009) Cdk1/Cdc28-dependent activation of the major triacylglycerol lipase Tgl4 in yeast links lipolysis to cell-cycle progression. Mol Cell 33(1):53-63 SGD PMID 19150427
  4. ↑ 4.0 4.1 Ubersax JA, et al. (2003) Targets of the cyclin-dependent kinase Cdk1. Nature 425(6960):859-64 SGD PMID 14574415 Cite error: Invalid <ref> tag; name "S000074306" defined multiple times with different content
  5. ↑ 5.0 5.1 submitted by Sepp D. Kohlwein on 2006-05-22
  6. ↑ submitted by Jeff Ubersax on 2004-01-29

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