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J Cell Sci. 2013 May 15;126(Pt 10):2198-212. doi: 10.1242/jcs.120493. Epub 2013 Mar 22.

The evolutionarily conserved protein CG9186 is associated with lipid droplets, required for their positioning and for fat storage.

Author information

  • 1Department of Molecular Developmental Biology, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.

Abstract

Lipid droplets (LDs) are specialized cell organelles for the storage of energy-rich lipids. Although lipid storage is a conserved feature of all cells and organisms, little is known about fundamental aspects of the cell biology of LDs, including their biogenesis, structural assembly and subcellular positioning, and the regulation of organismic energy homeostasis. We identified a novel LD-associated protein family, represented by the Drosophila protein CG9186 and its murine homolog MGI:1916082. In the absence of LDs, both proteins localize at the endoplasmic reticulum (ER). Upon lipid storage induction, they translocate to LDs using an evolutionarily conserved targeting mechanism that acts through a 60-amino-acid targeting motif in the center of the CG9186 protein. Overexpression of CG9186, and MGI:1916082, causes clustering of LDs in both tissue culture and salivary gland cells, whereas RNAi knockdown of CG9186 results in a reduction of LDs. Organismal RNAi knockdown of CG9186 results in a reduction in lipid storage levels of the fly. The results indicate that we identified the first members of a novel and evolutionarily conserved family of lipid storage regulators, which are also required to properly position LDs within cells.

KEYWORDS:

Drosophila melanogaster; Lipid droplets; Lipid metabolism; Organelle clustering; Organelle positioning

PMID:
23525007
[PubMed - indexed for MEDLINE]
PMCID:
PMC3880856
Free PMC Article
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