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Papers In Press, published online ahead of print September 13, 2007
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Biochemistry and Cell Biology, Stony Brook University, Stony Brook, NY 11794-5215
Corresponding Author: 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 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 association of adipose triglyceride lipase (ATGL) and TIP47 with lipid droplets, and also decreased lipid droplet association of several other unknown proteins. Transient expression of ADRP in two other cell lines also reduced lipid droplet association of catalytically-inactive ATGL. We conclude that reduced lipid droplet association of ATGL and/or other lipases may explain the decrease in TAG turnover observed in ADRP-expressing HEK 293 cells.
Revised on September 12, 2007
Accepted on September 12, 2007
Adipocyte differentiation-related protein reduces lipid droplet association of adipose triglyceride lipase and slows triacylglycerol turnover
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