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Originally published In Press as doi:10.1194/jlr.M700359-JLR200 on September 13, 2007

Papers In Press, published online ahead of print December 1, 2007
J. Lipid Res., doi:10.1194/jlr.M700359-JLR200
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Journal of Lipid Research, Vol. 48, 2751-2761, December 2007
Copyright © 2007 by American Society for Biochemistry and Molecular Biology

Adipocyte differentiation-related protein reduces the lipid droplet association of adipose triglyceride lipase and slows triacylglycerol turnoverboxs

Laura L. Listenberger*, Anne G. Ostermeyer-Fay*, Elysa B. Goldberg{dagger}, William J. Brown{dagger} and Deborah A. Brown1,*

* Department of Biochemistry and Cell Biology, Stony Brook University, Stony Brook, NY 11794
{dagger} Department of Molecular Biology and Genetics, Cornell University, Ithaca, NY 18483

boxs The online version of this article (available at http://www.jlr.org) contains supplementary data in the form of three figures.

Published, JLR Papers in Press, September 13, 2007.

1 To whom correspondence should be addressed. e-mail: deborah.brown{at}sunysb.edu

Although neutral lipid storage droplets are ubiquitous in eukaryotic cells, very little is known about how their synthesis and turnover are controlled. Adipocyte differentiation-related protein (ADRP; also known as adipophilin) is found on the surface of lipid droplets in most mammalian cell types. To learn how ADRP affects lipid storage, we stably expressed the protein in human embryonic kidney 293 (HEK 293) cells, which express little endogenous ADRP. As expected, ADRP was targeted to the surface of lipid droplets and caused an increase in triacylglycerol (TAG) mass under both basal and oleate-supplemented conditions. At least part of the increased mass resulted from a 50% decrease in the rate of TAG hydrolysis in ADRP-expressing cells. Furthermore, ADRP expression increased the fraction of total cellular TAG that was stored in lipid droplets. ADRP expression induced a striking decrease in the association of adipose triglyceride lipase (ATGL) and mannose-6-phosphate receptor tail-interacting protein of 47 kDa with lipid droplets and also decreased the lipid droplet association of several other unknown proteins. Transient expression of ADRP in two other cell lines also reduced the lipid droplet association of catalytically inactive ATGL. We conclude that the reduced lipid droplet association of ATGL and/or other lipases may explain the decrease in TAG turnover observed in ADRP-expressing HEK 293 cells.

Supplementary key words adipophilin • PAT proteins • ADRP • ADFP • PLIN2

Abbreviations: ADRP, adipocyte differentiation-related protein; ATGL, adipose triglyceride lipase; BHK, baby hamster kidney; GFP, green fluorescent protein; HEK 293, human embryonic kidney 293; HSL, hormone-sensitive lipase; TAG, triacylglycerol; TIP47, mannose-6-phosphate receptor tail-interacting protein of 47 kDa; 293/ADRP, ADRP-expressing HEK 293


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