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    Enzymes of sphingolipid metabolism in Drosophila melanogaster

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    Authors
    Acharya, Usha
    Acharya, Jairaj K.
    UMass Chan Affiliations
    Program in Gene Function and Expression
    Document Type
    Journal Article
    Publication Date
    2005-01-25
    Keywords
    Acyltransferases
    Alcohol Oxidoreductases
    Amidohydrolases
    Animals
    Ceramidases
    Ceramides
    Drosophila melanogaster
    Oxidoreductases
    Phosphotransferases (Alcohol Group Acceptor)
    Serine C-Palmitoyltransferase
    Sphingolipids
    Genetics and Genomics
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    Link to Full Text
    http://dx.doi.org/10.1007/s00018-004-4254-1
    Abstract
    Sphingolipids are important structural components of membranes that delimit the boundaries of cellular compartments, cells and organisms. They play an equally important role as second messengers, and transduce signals across or within the compartments they define to initiate physiological changes during development, differentiation and a host of other cellular events. For well over a century Drosophila melanogaster has served as a useful model organism to understand some of the fundamental tenets of development, differentiation and signaling in eukaryotic organisms. Directed approaches to study sphingolipid biology in Drosophila have been initiated only recently. Nevertheless, earlier phenotypic studies conducted on genes of unknown biochemical function have recently been recognized as mutants of enzymes of sphingolipid metabolism. Genome sequencing and annotation have aided the identification of homologs of recently discovered genes. Here we present an overview of studies on enzymes of the de novo sphingolipid biosynthetic pathway, known mutants and their phenotypic characterization in Drosophila.
    Source
    Cell Mol Life Sci. 2005 Jan;62(2):128-42. Link to article on publisher's site
    DOI
    10.1007/s00018-004-4254-1
    Permanent Link to this Item
    http://hdl.handle.net/20.500.14038/43922
    PubMed ID
    15666085
    Related Resources
    Link to Article in PubMed
    ae974a485f413a2113503eed53cd6c53
    10.1007/s00018-004-4254-1
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