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Journal Article

PERILIPIN-dependent control of lipid droplet structure and fat storage in Drosophila.

MPS-Authors
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Beller,  M.
Department of Molecular Developmental Biology, MPI for biophysical chemistry, Max Planck Society;

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Hsiao,  H.
Research Group of Bioanalytical Mass Spectrometry, MPI for biophysical chemistry, Max Planck Society;

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Urlaub,  H.
Research Group of Bioanalytical Mass Spectrometry, MPI for biophysical chemistry, Max Planck Society;

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Jäckle,  H.
Department of Molecular Developmental Biology, MPI for biophysical chemistry, Max Planck Society;

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Kühnlein,  R. P.
Research Group of Molecular Physiology, MPI for biophysical chemistry, Max Planck Society;

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587578-Suppl.pdf
(Supplementary material), 867KB

Citation

Beller, M., Bulankina, A. V., Hsiao, H., Urlaub, H., Jäckle, H., & Kühnlein, R. P. (2010). PERILIPIN-dependent control of lipid droplet structure and fat storage in Drosophila. Cell Metabolism, 12(5), 521-532. doi:10.1016/j.cmet.2010.10.001.


Cite as: https://hdl.handle.net/11858/00-001M-0000-0012-D4D1-0
Abstract
Lipid droplets are intracellular organelles enriched in adipose tissue that govern the body fat stores of animals. In mammals, members of the evolutionarily conserved PERILIPIN protein family are associated with the lipid droplet surface and participate in lipid homeostasis. Here, we show that Drosophila mutants lacking the PERILIPIN PLIN1 are hyperphagic and suffer from adult-onset obesity. PLIN1 is a central and Janus-faced component of fat metabolism. It provides barrier function to storage lipid breakdown and acts as a key factor of stimulated lipolysis by modulating the access of proteins to the lipid droplet surface. It also shapes lipid droplet structure, transforming unilocular into multilocular fat cells. We generated flies devoid of all PERILIPIN family members and show that they exhibit impaired yet functional body fat regulation. Our data reveal the existence of a basal and possibly ancient lipid homeostasis system.