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Originally published In Press as doi:10.1074/jbc.M204707200 on June 20, 2002

J. Biol. Chem., Vol. 277, Issue 36, 32466-32472, September 6, 2002
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Transcriptional Profiling Identifies Two Members of the ATP-binding Cassette Transporter Superfamily Required for Sterol Uptake in Yeast*

Lisa J. WilcoxDagger §, Dina A. BalderesDagger , Brook WhartonDagger , Arthur H. TinkelenbergDagger , Govinda Rao, and Stephen L. SturleyDagger ||**

From the Dagger  Institute of Human Nutrition and || Department of Pediatrics, Columbia University College of Physicians and Surgeons, New York, New York 10032 and  Affymetrix, Inc., Santa Clara, California 95051

In contrast to lipoprotein-mediated sterol uptake, free sterol influx by eukaryotic cells is poorly understood. To identify components of non-lipoprotein-mediated sterol uptake, we utilized strains of Saccharomyces cerevisiae that accumulate exogenous sterol due to a neomorphic mutation in the transcription factor, UPC2. Two congenic upc2-1 strains, differing quantitatively in aerobic sterol uptake due to a modifying mutation in the HAP1 transcription factor, were compared using DNA microarrays. We identified 9 genes as responsive to UPC2 that were also induced under anaerobiosis, when sterol uptake is essential. Deletion mutants in these genes were assessed for sterol influx in the upc2-1 background. UPC2 itself was up-regulated under these conditions and was required for aerobic sterol influx. Deletion of the ATP-binding cassette transporters YOR011w (AUS1) or PDR11, or a putative cell wall protein encoded by DAN1, significantly reduced sterol influx. Sodium azide and vanadate inhibited sterol uptake, consistent with the participation of ATP-binding cassette transporters. We hypothesized that the physiological role of Aus1p and Pdr11p is to mediate sterol uptake when sterol biosynthesis is compromised. Accordingly, expression of AUS1 or PDR11 was required for anaerobic growth and sterol uptake. We proposed similar molecules may be important components of sterol uptake in all eukaryotes.

* This work was supported in part by the Ara Parseghian Medical Research Foundation (to S. L. S.), the Hirschl/Weil-Caulier Trust (to S. L. S.), and National Institutes of Health Grant DK54320 (to S. L. S.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ Supported by a fellowship from the Heart and Stroke Foundation of Canada.

** Established Investigator of the American Heart Association. To whom correspondence and reprint requests should be addressed: Institute of Human Nutrition, Columbia University College of Physicians and Surgeons, 650 W. 168th St., New York, NY 10032. Tel.: 212-305-6304; Fax: 212-305-3079; E-mail: sls37@columbia.edu.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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