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dc.contributor.authorAcharya, Usha
dc.contributor.authorMowen, Michael Beth
dc.contributor.authorNagashima, Kunio
dc.contributor.authorAcharya, Jairaj K.
dc.date2022-08-11T08:10:15.000
dc.date.accessioned2022-08-23T17:01:06Z
dc.date.available2022-08-23T17:01:06Z
dc.date.issued2004-02-11
dc.date.submitted2011-04-19
dc.identifier.citationProc Natl Acad Sci U S A. 2004 Feb 17;101(7):1922-6. Epub 2004 Feb 9. <a href="http://dx.doi.org/10.1073/pnas.0308693100">Link to article on publisher's site</a>
dc.identifier.issn0027-8424 (Linking)
dc.identifier.doi10.1073/pnas.0308693100
dc.identifier.pmid14769922
dc.identifier.urihttp://hdl.handle.net/20.500.14038/43933
dc.description.abstractTransgenic expression of ceramidase suppresses retinal degeneration in Drosophila arrestin and phospholipase C mutants. Here, we show that expression of ceramidase facilitates the dissolution of incompletely formed and inappropriately located elements of rhabdomeric membranes in ninaE(I17) mutants lacking the G protein receptor Rh1 in R1-R6 photoreceptor cells. Ceramidase expression facilitates the endocytic turnover of Rh1. Although ceramidase expression aids the removal of internalized rhodopsin, it does not affect the turnover of Rh1 in photoreceptors maintained in dark, where Rh1 is not activated and thus has a slower turnover and a long half-life. Therefore, the phenotypic consequence of ceramidase expression in photoreceptors is caused by facilitation of endocytosis. This study provides mechanistic insight into the sphingolipid biosynthetic pathway-mediated modulation of endocytosis and suppression of retinal degeneration.
dc.language.isoen_US
dc.relation<a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=14769922&dopt=Abstract">Link to Article in PubMed</a>
dc.relation.urlhttp://dx.doi.org/10.1073/pnas.0308693100
dc.subjectAmidohydrolases
dc.subjectAnimals
dc.subjectAnimals, Genetically Modified
dc.subjectCell Membrane
dc.subjectCeramidases
dc.subjectDarkness
dc.subjectDrosophila Proteins
dc.subjectDrosophila melanogaster
dc.subject*Endocytosis
dc.subjectEye Proteins
dc.subjectHalf-Life
dc.subjectLigands
dc.subjectLight
dc.subjectMutation
dc.subjectPhotoreceptor Cells, Invertebrate
dc.subjectReceptors, G-Protein-Coupled
dc.subjectRetinal Degeneration
dc.subjectRhodopsin
dc.subjectGenetics and Genomics
dc.titleCeramidase expression facilitates membrane turnover and endocytosis of rhodopsin in photoreceptors
dc.typeJournal Article
dc.source.journaltitleProceedings of the National Academy of Sciences of the United States of America
dc.source.volume101
dc.source.issue7
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/pgfe_pp/145
dc.identifier.contextkey1946800
html.description.abstract<p>Transgenic expression of ceramidase suppresses retinal degeneration in Drosophila arrestin and phospholipase C mutants. Here, we show that expression of ceramidase facilitates the dissolution of incompletely formed and inappropriately located elements of rhabdomeric membranes in ninaE(I17) mutants lacking the G protein receptor Rh1 in R1-R6 photoreceptor cells. Ceramidase expression facilitates the endocytic turnover of Rh1. Although ceramidase expression aids the removal of internalized rhodopsin, it does not affect the turnover of Rh1 in photoreceptors maintained in dark, where Rh1 is not activated and thus has a slower turnover and a long half-life. Therefore, the phenotypic consequence of ceramidase expression in photoreceptors is caused by facilitation of endocytosis. This study provides mechanistic insight into the sphingolipid biosynthetic pathway-mediated modulation of endocytosis and suppression of retinal degeneration.</p>
dc.identifier.submissionpathpgfe_pp/145
dc.contributor.departmentProgram in Gene Function and Expression
dc.source.pages1922-6


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