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

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

Research output: Contribution to journalArticlepeer-review

213 Citations (Scopus)


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
Issue number5
Publication statusPublished - 05-03-2001
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Cell Biology


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