J. Lipid Res.
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A more recent version of this article appeared on April 1, 2003

Papers In Press, published online ahead of print January 16, 2003
J. Lipid Res., doi:10.1194/jlr.C200021-JLR200
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Submitted on November 29, 2002
Revised on January 3, 2003
Accepted on January 8, 2003

Lipid droplet targeting domains of adipophilin

James L. McManaman, William Zabaronick, Jerome Schaack, and David J. Orlicky

Obstetrics and Gynecology, University of Colorado Health Sciences Center, Denver, CO 80262

Corresponding Author: jim.mcmanaman{at}uchsc.edu

Adipophilin (ADPH), a prominent protein component of lipid storage droplets (LSDs), is postulated to be necessary for the formation and cellular function of these structures. The presence of significant sequence similarities within a ~ 100 amino acid region of the N-terminal portions of ADPH and related LSD binding proteins, Perilipin and TIP47, has implicated this region, known as the "PAT domain", in LSD targeting. Here we investigate the role of the "PAT domain" in targeting ADPH to LSDs by expressing this region, as well as selected N- and C-terminal truncations of mouse ADPH, in COS cells as epitope-tagged fusion proteins. Our studies show that truncations lacking either the "PAT domain" or the C-terminal half of ADPH both correctly targeted LSDs and increased the LSD content of transfected cells. Neither the "PAT domain", nor the C-terminal half of ADPH, appeared to target LSDs or affect LSD number. Instead, targeting fragments encompassed a putative a-helical region between amino acids 189-205, implicating this region in both LSD targeting and regulation of LSD formation.


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