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© The Rockefeller University Press,
0021-9525/2001//1079 $5.00
The Journal of Cell Biology, Volume 152, Number 5,
, 2001 1079-1086
Original Article |
Caveolin-2 Is Targeted to Lipid Droplets, a New "Membrane Domain" in the Cell
tfujimot{at}med.nagoya-u.ac.jp
Caveolin-1 and -2 constitute a framework of caveolae in nonmuscle cells. In the present study, we showed that caveolin-2, especially its β isoform, is targeted to the surface of lipid droplets (LD) by immunofluorescence and immunoelectron microscopy, and by subcellular fractionation. Brefeldin A treatment induced further accumulation of caveolin-2 along with caveolin-1 in LD. Analysis of mouse caveolin-2 deletion mutants revealed that the central hydrophobic domain (residues 87–119) and the NH2-terminal (residues 70–86) and COOH-terminal (residues 120–150) hydrophilic domains are all necessary for the localization in LD. The NH2- and COOH-terminal domains appeared to be related to membrane binding and exit from ER, respectively, implying that caveolin-2 is synthesized and transported to LD as a membrane protein. In conjunction with recent findings that LD contain unesterified cholesterol and raft proteins, the result implies that the LD surface may function as a membrane domain. It also suggests that LD is related to trafficking of lipid molecules mediated by caveolins.
Key Words: lipid droplet caveolin-2 caveolin-1 membrane domain brefeldin A
© 2001 The Rockefeller University Press
Dr. Nomura's current address is Department of Anatomy, Hiroshima University School of Medicine, Hiroshima 734-8551, Japan.Abbreviations used in this paper: BFA, brefeldin A; EGFP, enhanced green fluorescent protein; LD, lipid droplets; NRK, normal rat kidney; OA, oleic acid.
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