Caveolin-2 is targeted to lipid droplets, a new "membrane domain" in the cell

Toyoshi Fujimoto, Hiroshi Kogo, Kimiko Ishiguro, Kumi Tauchi, Ryuji Nomura

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203 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)1079-1085
Number of pages7
JournalJournal of Cell Biology
Volume152
Issue number5
DOIs
Publication statusPublished - 05-03-2001

All Science Journal Classification (ASJC) codes

  • Cell Biology

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    Fujimoto, T., Kogo, H., Ishiguro, K., Tauchi, K., & Nomura, R. (2001). Caveolin-2 is targeted to lipid droplets, a new "membrane domain" in the cell. Journal of Cell Biology, 152(5), 1079-1085. https://doi.org/10.1083/jcb.152.5.1079