Source:http://linkedlifedata.com/resource/pubmed/id/21071438
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
2011-1-10
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pubmed:abstractText |
In the yeast Saccharomyces cerevisiae, triacylglycerol mobilization for phospholipid synthesis occurs during growth resumption from stationary phase, and this metabolism is essential in the absence of de novo fatty acid synthesis. In this work, we provide evidence that DGK1-encoded diacylglycerol kinase activity is required to convert triacylglycerol-derived diacylglycerol to phosphatidate for phospholipid synthesis. Cells lacking diacylglycerol kinase activity (e.g. dgk1? mutation) failed to resume growth in the presence of the fatty acid synthesis inhibitor cerulenin. Lipid analysis data showed that dgk1? mutant cells did not mobilize triacylglycerol for membrane phospholipid synthesis and accumulated diacylglycerol. The dgk1? phenotypes were partially complemented by preventing the formation of diacylglycerol by the PAH1-encoded phosphatidate phosphatase and by channeling diacylglycerol to phosphatidylcholine via the Kennedy pathway. These observations, coupled to an inhibitory effect of dioctanoyl-diacylglycerol on the growth of wild type cells, indicated that diacylglycerol kinase also functions to alleviate diacylglycerol toxicity.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Cerulenin,
http://linkedlifedata.com/resource/pubmed/chemical/Choline,
http://linkedlifedata.com/resource/pubmed/chemical/Diacylglycerol Kinase,
http://linkedlifedata.com/resource/pubmed/chemical/Diglycerides,
http://linkedlifedata.com/resource/pubmed/chemical/HSD1 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidate Phosphatase,
http://linkedlifedata.com/resource/pubmed/chemical/Phospholipids,
http://linkedlifedata.com/resource/pubmed/chemical/Repressor Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/SMP2 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
1083-351X
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:day |
14
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pubmed:volume |
286
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1464-74
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pubmed:dateRevised |
2011-4-19
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pubmed:meshHeading |
pubmed-meshheading:21071438-Cerulenin,
pubmed-meshheading:21071438-Choline,
pubmed-meshheading:21071438-Diacylglycerol Kinase,
pubmed-meshheading:21071438-Diglycerides,
pubmed-meshheading:21071438-Gene Deletion,
pubmed-meshheading:21071438-Phosphatidate Phosphatase,
pubmed-meshheading:21071438-Phospholipids,
pubmed-meshheading:21071438-Repressor Proteins,
pubmed-meshheading:21071438-Saccharomyces cerevisiae,
pubmed-meshheading:21071438-Saccharomyces cerevisiae Proteins
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pubmed:year |
2011
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pubmed:articleTitle |
DGK1-encoded diacylglycerol kinase activity is required for phospholipid synthesis during growth resumption from stationary phase in Saccharomyces cerevisiae.
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pubmed:affiliation |
Department of Food Science and Rutgers Center for Lipid Research, Rutgers University, New Brunswick, New Jersey 08901, USA.
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pubmed:publicationType |
Journal Article,
Research Support, N.I.H., Extramural
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