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Molecular & Cellular Proteomics 5:1082-1094, 2006.
© 2006 by The American Society for Biochemistry and Molecular Biology, Inc.

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Research

Characterization of the Drosophila Lipid Droplet Subproteome^*,S

Mathias Beller^,, Dietmar Riedel^¶, Lothar Jänsch^||, Guido Dieterich^||, Jürgen Wehland^||, Herbert Jäckle and Ronald P. Kühnlein^,**

From the Abteilung Molekulare Entwicklungsbiologie and ^¶ Abteilung Neurobiologie, Max-Planck-Institut für biophysikalische Chemie, Am Fassberg 11, 37077 Göttingen, Germany ^|| Abteilung Zellbiologie, Gesellschaft für Biotechnologische Forschung GBF, Mascheroder Weg 1, 38124 Braunschweig, Germany

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.

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