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Published 5 January 2004. doi:10.1083/jcb.200303037
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 164, Number 1, 69-78
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Article

 Role of the hydrophobic domain in targeting caveolin-1 to lipid droplets

Anne G. Ostermeyer1, Lynne T. Ramcharan1, Youchun Zeng2, Douglas M. Lublin2 and Deborah A. Brown1

1 Department of Biochemistry and Cell Biology, State University of New York at Stony Brook, Stony Brook, NY 11794
2 Department of Pathology, Washington University School of Medicine, St. Louis, MO 63110

Address correspondence to D.A. Brown, Department of Biochemistry and Cell Biology, State University of New York at Stony Brook, Stony Brook, NY 11794-5215. Tel.: (631) 632-8563. Fax: (631) 632-8575. email: deborah.brown{at}sunysb.edu

Although caveolins normally reside in caveolae, they can accumulate on the surface of cytoplasmic lipid droplets (LDs). Here, we first provided support for our model that overaccumulation of caveolins in the endoplasmic reticulum (ER) diverts the proteins to nascent LDs budding from the ER. Next, we found that a mutant H-Ras, present on the cytoplasmic surface of the ER but lacking a hydrophobic peptide domain, did not accumulate on LDs. We used the fact that wild-type caveolin-1 accumulates in LDs after brefeldin A treatment or when linked to an ER retrieval motif to search for mutants defective in LD targeting. The hydrophobic domain, but no specific sequence therein, was required for LD targeting of caveolin-1. Certain Leu insertions blocked LD targeting, independently of hydrophobic domain length, but dependent on their position in the domain. We propose that proper packing of putative hydrophobic helices may be required for LD targeting of caveolin-1.

Key Words: secondary protein structure; caveolins; hydrophobicity; protein transport; cell membrane

Abbreviations used in this paper: ADRP, adipocyte differentiation related protein; BFA, brefeldin A; DTAF, dichlorotriazinylaminofluorescein; FRT, Fischer rat thyroid; GAM, goat anti–mouse Ig(G + M); GAR, goat anti–rabbit IgG; GBV-B, GB virus-B; HCV, hepatitis C virus; IF, indirect immunofluorescence microscopy; LD, lipid droplet; PLAP, placental AP.


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