2.50
Hdl Handle:
http://hdl.handle.net/10033/12901
Title:
Characterization of the Drosophila lipid droplet subproteome.
Authors:
Beller, Mathias; Riedel, Dietmar; Jänsch, Lothar ( 0000-0002-5655-1181 ) ; Dieterich, Guido; Wehland, Jürgen; Jäckle, Herbert; Kühnlein, Ronald P
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
Issue Date:
1-Jun-2006
URI:
http://hdl.handle.net/10033/12901
DOI:
10.1074/mcp.M600011-MCP200
PubMed ID:
16543254
Type:
Article
Language:
en
ISSN:
1535-9476
Appears in Collections:
Publications of Dept. Cell Biology (ZB)

Full metadata record

DC FieldValue Language
dc.contributor.authorBeller, Mathiasen
dc.contributor.authorRiedel, Dietmaren
dc.contributor.authorJänsch, Lotharen
dc.contributor.authorDieterich, Guidoen
dc.contributor.authorWehland, Jürgenen
dc.contributor.authorJäckle, Herberten
dc.contributor.authorKühnlein, Ronald Pen
dc.date.accessioned2007-07-23T14:10:28Zen
dc.date.available2007-07-23T14:10:28Zen
dc.date.issued2006-06-01en
dc.identifier.citationMol. Cell Proteomics 2006, 5(6):1082-94en
dc.identifier.issn1535-9476en
dc.identifier.pmid16543254en
dc.identifier.doi10.1074/mcp.M600011-MCP200en
dc.identifier.urihttp://hdl.handle.net/10033/12901en
dc.description.abstractLipid 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.en
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dc.titleCharacterization of the Drosophila lipid droplet subproteome.en
dc.typeArticleen
dc.format.digYESen

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