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J. Biol. Chem., Vol. 279, Issue 50, 52399-52405, December 10, 2004

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Physical Association between the Adipocyte Fatty Acid-binding Protein and Hormone-sensitive Lipase

A FLUORESCENCE RESONANCE ENERGY TRANSFER ANALYSIS^*

Anne J. Smith, Mark A. Sanders, Brian R. Thompson, Constantine Londos¶, Fredric B. Kraemer||, and David A. Bernlohr**

From the Department of Biochemistry, Molecular Biology and Biophysics, The University of Minnesota, Minneapolis, Minnesota 55455, The Imaging Center, University of Minnesota, St. Paul, Minnesota 55108, ^¶Membrane Regulation Section, NIDDK, National Institutes of Health, Bethesda, Maryland 20892, and ^||Division of Endocrinology, Department of Medicine, Stanford University, Stanford, California 94305, and Veterans Administration Palo Alto Health Care System, Palo Alto, California 94304

Previous in vitro studies have established that hormone sensitive lipase (HSL) and adipocyte fatty acid-binding protein (AFABP) form a physical complex that presumably positions the FABP to accept a product fatty acid generated during catalysis. To assess AFABP-HSL interaction within a cellular context, we have used lipocytes derived from 293 cells (C8PA cells) and examined physical association using fluorescence resonance energy transfer. Transfection of C8PA cells with cyan fluorescent protein (CFP)-HSL, yellow fluorescent protein (YFP)-adipocyte FABP, or YFP-liver FABP revealed that under basal conditions each protein was cytoplasmic. In the presence of 20 µM forskolin, CFP-HSL translocated to the triacylglycerol droplet, coincident with BODIPY-FA labeled depots. Fluorescence resonance energy transfer analysis demonstrated that CFP-HSL associated with YFP-adipocyte FABP in both basal and forskolin-treated cells. In contrast, little if any fluorescence resonance energy transfer could be detected between CFP-HSL and YFP-liver FABP. These results suggest that a pre-lipolysis complex containing at least AFABP and HSL exists and that the complex translocates to the surface of the lipid droplet.

Received for publication, September 8, 2004

^* This work was supported by National Institutes of Health Grant DK 53189 and by the Minnesota Obesity Center (to D. A. B.) and the Research Service of the Department of Veterans Affairs and National Institutes of Health Grant DK 46942 (to F. B. K.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

^** To whom correspondence should be addressed: Dept. of Biochemistry, Molecular Biology, and Biophysics, The University of Minnesota, 321 Church St. SE, Minneapolis, MN 55455. Tel.: 612-624-2712; Fax: 612-625-2163; E-mail: bernl001{at}umn.edu.

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