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Published online 3 April 2006. doi:10.1083/jcb.200510084
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 173, Number 1, 107-119
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Article

Nonvesicular sterol movement from plasma membrane to ER requires oxysterol-binding protein–related proteins and phosphoinositides



Sumana Raychaudhuri1, Young Jun Im2, James H. Hurley2, and William A. Prinz1

1 Laboratory of Cell Biochemistry and Biology and 2 Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, United States Department of Health and Human Services, Bethesda, MD 20892

Correspondence to William A Prinz: wprinz{at}helix.nih.gov

Sterols are moved between cellular membranes by nonvesicular pathways whose functions are poorly understood. In yeast, one such pathway transfers sterols from the plasma membrane (PM) to the endoplasmic reticulum (ER). We show that this transport requires oxysterol-binding protein (OSBP)–related proteins (ORPs), which are a large family of conserved lipid-binding proteins. We demonstrate that a representative member of this family, Osh4p/Kes1p, specifically facilitates the nonvesicular transfer of cholesterol and ergosterol between membranes in vitro. In addition, Osh4p transfers sterols more rapidly between membranes containing phosphoinositides (PIPs), suggesting that PIPs regulate sterol transport by ORPs. We confirmed this by showing that PM to ER sterol transport slows dramatically in mutants with conditional defects in PIP biosynthesis. Our findings argue that ORPs move sterols among cellular compartments and that sterol transport and intracellular distribution are regulated by PIPs.

Y.J. Im's present address is Dept. of Life Science, Gwangju Institute of Science and Technology, Gwangju City, 500-712, South Korea.

Abbreviations used in this paper: ACAT, acyl-coenzyme A:cholesterol acyltransferase; DAG, dioleoyl glycerol; DOPC, dioleoyl phosphatidyl choline; ORP, OSBP-related protein; OSBP, oxysterol-binding protein; PC, dipalmitoyl phosphatiylcholine; PH, pleckstrin homologue; PI, phosphatidylinositol; PI(4,5)P2, phosphatidylinositol(4,5) bisphosphate; PIP, phosphoinositide; PM, plasma membrane; pmol, picomols; PS, phosphatidylserine; Psd, PS decarboxylase; TAG, triolein.


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