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    Characterization of the Drosophila lipid droplet subproteome.

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    Authors
    Beller, Mathias
    Riedel, Dietmar
    Jänsch, Lothar cc
    Dieterich, Guido
    Wehland, Jürgen
    Jäckle, Herbert
    Kühnlein, Ronald P
    Issue Date
    2006-06-01
    
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    Abstract
    Lipid storage droplets are universal organelles essential for the cellular and organismal lipometabolism including energy homeostasis. Despite their apparently simple design they are proposed to participate in a growing number of cellular processes, raising the question to what extent the functional multifariousness is reflected by a complex organellar proteome composition. Here we present 248 proteins identified in a subproteome analysis using lipid storage droplets of Drosophila melanogaster fat body tissue. In addition to previously known lipid droplet-associated PAT (Perilipin, ADRP, and TIP47) domain proteins and homologues of several mammalian lipid droplet proteins, this study identified a number of proteins of diverse biological function, including intracellular trafficking supportive of the dynamic and multifaceted character of these organelles. We performed intracellular localization studies on selected newly identified subproteome members both in tissue culture cells and in fat body cells directly. The results suggest that the lipid droplets of fat body cells are of combinatorial protein composition. We propose that subsets of lipid droplets within single cells are characterized by a protein "zip code," which reflects functional differences or specific metabolic states.
    Citation
    Mol. Cell Proteomics 2006, 5(6):1082-94
    URI
    http://hdl.handle.net/10033/12901
    DOI
    10.1074/mcp.M600011-MCP200
    PubMed ID
    16543254
    Type
    Article
    Language
    en
    ISSN
    1535-9476
    ae974a485f413a2113503eed53cd6c53
    10.1074/mcp.M600011-MCP200
    Scopus Count
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