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    Ceramidase expression facilitates membrane turnover and endocytosis of rhodopsin in photoreceptors

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    Authors
    Acharya, Usha
    Mowen, Michael Beth
    Nagashima, Kunio
    Acharya, Jairaj K.
    UMass Chan Affiliations
    Program in Gene Function and Expression
    Document Type
    Journal Article
    Publication Date
    2004-02-11
    Keywords
    Amidohydrolases
    Animals
    Animals, Genetically Modified
    Cell Membrane
    Ceramidases
    Darkness
    Drosophila Proteins
    Drosophila melanogaster
    *Endocytosis
    Eye Proteins
    Half-Life
    Ligands
    Light
    Mutation
    Photoreceptor Cells, Invertebrate
    Receptors, G-Protein-Coupled
    Retinal Degeneration
    Rhodopsin
    Genetics and Genomics
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    Link to Full Text
    http://dx.doi.org/10.1073/pnas.0308693100
    Abstract
    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.
    Source
    Proc Natl Acad Sci U S A. 2004 Feb 17;101(7):1922-6. Epub 2004 Feb 9. Link to article on publisher's site
    DOI
    10.1073/pnas.0308693100
    Permanent Link to this Item
    http://hdl.handle.net/20.500.14038/43933
    PubMed ID
    14769922
    Related Resources
    Link to Article in PubMed
    ae974a485f413a2113503eed53cd6c53
    10.1073/pnas.0308693100
    Scopus Count
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