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dc.contributor.authorYuan, Changqing
dc.contributor.authorRao, Raghavendra Pralhada
dc.contributor.authorJesmin, Nahid
dc.contributor.authorBamba, Takeshi
dc.contributor.authorNagashima, Kunio
dc.contributor.authorPascual, Alberto
dc.contributor.authorPreat, Thomas
dc.contributor.authorFukusaki, Eiichiro
dc.contributor.authorAcharya, Usha
dc.contributor.authorAcharya, Jairaj K.
dc.date2022-08-11T08:10:16.000
dc.date.accessioned2022-08-23T17:01:41Z
dc.date.available2022-08-23T17:01:41Z
dc.date.issued2011-01-15
dc.date.submitted2011-04-19
dc.identifier.citationMol Biol Cell. 2011 Jan 1;22(1):33-43. Epub 2010 Dec 9. <a href="http://dx.doi.org/10.1091/mbc.E10-05-0453">Link to article on publisher's site</a>
dc.identifier.issn1059-1524 (Linking)
dc.identifier.doi10.1091/mbc.E10-05-0453
dc.identifier.pmid21148295
dc.identifier.urihttp://hdl.handle.net/20.500.14038/44060
dc.description.abstractCeramidases catalyze the conversion of ceramide to sphingosine. They are acylaminohydrolases that catalyze the deacylation of the amide-linked saturated fatty acid from ceramide to generate sphingosine. They also catalyze the reverse reaction of ceramide biosynthesis using sphingosine and fatty acid. In mammals, different proteins catalyze these reactions while individually exhibiting optimal activity over a narrow pH range and have been accordingly called acid, neutral, and alkaline ceramidases. Several genes encode for variants of alkaline ceramidase in mammals. Brainwashing (Bwa) is the only putative alkaline ceramidase homologue present in Drosophila. In this study we have demonstrated that BWA does not exhibit ceramidase activity and that bwa null mutants display no loss of ceramidase activity. Instead, the neutral ceramidase gene CDase encodes the protein that is responsible for all measurable ceramidase activity in Drosophila. Our studies show strong genetic interaction of Bwa with CDase and the Drosophila ceramide kinase gene (DCERK). We show that, although BWA is unlikely to be a ceramidase, it is a regulator of sphingolipid flux in Drosophila. Bwa exhibits strong genetic interaction with other genes coding for ceramide-metabolizing enzymes. This interaction might partly explain its original identification as a ceramidase.
dc.language.isoen_US
dc.relation<a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=21148295&dopt=Abstract">Link to Article in PubMed</a>
dc.subjectDrosophila Proteins
dc.subjectCeramidases
dc.subjectAmidohydrolases
dc.subjectGenetics and Genomics
dc.titleCDase is a pan-ceramidase in Drosophila
dc.typeJournal Article
dc.source.journaltitleMolecular biology of the cell
dc.source.volume22
dc.source.issue1
dc.identifier.legacyfulltexthttps://escholarship.umassmed.edu/cgi/viewcontent.cgi?article=1035&amp;context=pgfe_pp&amp;unstamped=1
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/pgfe_pp/35
dc.identifier.contextkey1946688
refterms.dateFOA2022-08-23T17:01:41Z
html.description.abstract<p>Ceramidases catalyze the conversion of ceramide to sphingosine. They are acylaminohydrolases that catalyze the deacylation of the amide-linked saturated fatty acid from ceramide to generate sphingosine. They also catalyze the reverse reaction of ceramide biosynthesis using sphingosine and fatty acid. In mammals, different proteins catalyze these reactions while individually exhibiting optimal activity over a narrow pH range and have been accordingly called acid, neutral, and alkaline ceramidases. Several genes encode for variants of alkaline ceramidase in mammals. Brainwashing (Bwa) is the only putative alkaline ceramidase homologue present in Drosophila. In this study we have demonstrated that BWA does not exhibit ceramidase activity and that bwa null mutants display no loss of ceramidase activity. Instead, the neutral ceramidase gene CDase encodes the protein that is responsible for all measurable ceramidase activity in Drosophila. Our studies show strong genetic interaction of Bwa with CDase and the Drosophila ceramide kinase gene (DCERK). We show that, although BWA is unlikely to be a ceramidase, it is a regulator of sphingolipid flux in Drosophila. Bwa exhibits strong genetic interaction with other genes coding for ceramide-metabolizing enzymes. This interaction might partly explain its original identification as a ceramidase.</p>
dc.identifier.submissionpathpgfe_pp/35
dc.contributor.departmentProgram in Gene Function and Expression
dc.source.pages33-43


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