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Journal Article

OSBP-related protein 2 is a sterol receptor on lipid droplets that regulates the metabolism of neutral lipids

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Suchanek,  Monika
Max Planck Institute of Molecular Cell Biology and Genetics, Max Planck Society;

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Spandl,  Johanna
Max Planck Institute of Molecular Cell Biology and Genetics, Max Planck Society;

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Thiele,  Christoph
Max Planck Institute of Molecular Cell Biology and Genetics, Max Planck Society;

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Citation

Hynynen, R., Suchanek, M., Spandl, J., Back, N., Thiele, C., & Olkkonen, V. M. (2009). OSBP-related protein 2 is a sterol receptor on lipid droplets that regulates the metabolism of neutral lipids. Journal of Lipid Research, 50(7), 1305-1315.


Cite as: https://hdl.handle.net/21.11116/0000-0001-0D5E-9
Abstract
Oxysterol binding protein-related protein 2 (ORP2) is a member of the oxysterol binding protein family, previously shown to bind 25-hydroxycholesterol and implicated in cellular cholesterol metabolism. We show here that ORP2 also binds 22(R)-hydroxycholesterol [22(R)OHC], 7-ketocholesterol, and cholesterol, with 22(R)OHC being the highest affinity ligand of ORP2 (K(d) 1.4 x 10(-8) M). We report the localization of ORP2 on cytoplasmic lipid droplets (LDs) and its function in neutral lipid metabolism using the human A431 cell line as a model. The ORP2 LD association depends on sterol binding: Treatment with 5 microM 22(R)OHC inhibits the LD association, while a mutant defective in sterol binding is constitutively LD bound. Silencing of ORP2 using RNA interference slows down cellular triglyceride hydrolysis. Furthermore, ORP2 silencing increases the amount of [(14)C]cholesteryl esters but only under conditions in which lipogenesis and LD formation are enhanced by treatment with oleic acid. The results identify ORP2 as a sterol receptor present on LD and provide evidence for its role in the regulation of neutral lipid metabolism, possibly as a factor that integrates the cellular metabolism of triglycerides with that of cholesterol.