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http://purl.uniprot.org/citations/22633490http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/22633490http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/22633490http://www.w3.org/2000/01/rdf-schema#comment"Sphingosine 1-phosphate (S1P) functions not only as a bioactive lipid molecule, but also as an important intermediate of the sole sphingolipid-to-glycerolipid metabolic pathway. However, the precise reactions and the enzymes involved in this pathway remain unresolved. We report here that yeast HFD1 and the Sjögren-Larsson syndrome (SLS)-causative mammalian gene ALDH3A2 are responsible for conversion of the S1P degradation product hexadecenal to hexadecenoic acid. The absence of ALDH3A2 in CHO-K1 mutant cells caused abnormal metabolism of S1P/hexadecenal to ether-linked glycerolipids. Moreover, we demonstrate that yeast Faa1 and Faa4 and mammalian ACSL family members are acyl-CoA synthetases involved in the sphingolipid-to-glycerolipid metabolic pathway and that hexadecenoic acid accumulates in Δfaa1 Δfaa4 mutant cells. These results unveil the entire S1P metabolic pathway: S1P is metabolized to glycerolipids via hexadecenal, hexadecenoic acid, hexadecenoyl-CoA, and palmitoyl-CoA. From our results we propose a possibility that accumulation of the S1P metabolite hexadecenal contributes to the pathogenesis of SLS."xsd:string
http://purl.uniprot.org/citations/22633490http://purl.org/dc/terms/identifier"doi:10.1016/j.molcel.2012.04.033"xsd:string
http://purl.uniprot.org/citations/22633490http://purl.org/dc/terms/identifier"doi:10.1016/j.molcel.2012.04.033"xsd:string
http://purl.uniprot.org/citations/22633490http://purl.uniprot.org/core/author"Abe K."xsd:string
http://purl.uniprot.org/citations/22633490http://purl.uniprot.org/core/author"Abe K."xsd:string
http://purl.uniprot.org/citations/22633490http://purl.uniprot.org/core/author"Naganuma T."xsd:string
http://purl.uniprot.org/citations/22633490http://purl.uniprot.org/core/author"Naganuma T."xsd:string
http://purl.uniprot.org/citations/22633490http://purl.uniprot.org/core/author"Nakahara K."xsd:string
http://purl.uniprot.org/citations/22633490http://purl.uniprot.org/core/author"Nakahara K."xsd:string
http://purl.uniprot.org/citations/22633490http://purl.uniprot.org/core/author"Kitamura T."xsd:string
http://purl.uniprot.org/citations/22633490http://purl.uniprot.org/core/author"Kitamura T."xsd:string
http://purl.uniprot.org/citations/22633490http://purl.uniprot.org/core/author"Kihara A."xsd:string
http://purl.uniprot.org/citations/22633490http://purl.uniprot.org/core/author"Kihara A."xsd:string
http://purl.uniprot.org/citations/22633490http://purl.uniprot.org/core/author"Ohkuni A."xsd:string
http://purl.uniprot.org/citations/22633490http://purl.uniprot.org/core/author"Ohkuni A."xsd:string
http://purl.uniprot.org/citations/22633490http://purl.uniprot.org/core/author"Ohno Y."xsd:string
http://purl.uniprot.org/citations/22633490http://purl.uniprot.org/core/author"Ohno Y."xsd:string
http://purl.uniprot.org/citations/22633490http://purl.uniprot.org/core/author"Zoeller R.A."xsd:string
http://purl.uniprot.org/citations/22633490http://purl.uniprot.org/core/author"Zoeller R.A."xsd:string
http://purl.uniprot.org/citations/22633490http://purl.uniprot.org/core/date"2012"xsd:gYear
http://purl.uniprot.org/citations/22633490http://purl.uniprot.org/core/date"2012"xsd:gYear
http://purl.uniprot.org/citations/22633490http://purl.uniprot.org/core/name"Mol. Cell"xsd:string
http://purl.uniprot.org/citations/22633490http://purl.uniprot.org/core/name"Mol. Cell"xsd:string