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 journalArticle

196 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

Fingerprint

Caveolin 2
Membranes
Caveolin 1
Caveolins
Brefeldin A
Caveolae
Immunoelectron Microscopy
Lipid Droplets
Fluorescence Microscopy
Protein Isoforms
Membrane Proteins
Cholesterol
Lipids

All Science Journal Classification (ASJC) codes

  • Cell Biology

Cite this

Fujimoto, Toyoshi ; Kogo, Hiroshi ; Ishiguro, Kimiko ; Tauchi, Kumi ; Nomura, Ryuji. / Caveolin-2 is targeted to lipid droplets, a new "membrane domain" in the cell. In: Journal of Cell Biology. 2001 ; Vol. 152, No. 5. pp. 1079-1085.
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Caveolin-2 is targeted to lipid droplets, a new "membrane domain" in the cell. / Fujimoto, Toyoshi; Kogo, Hiroshi; Ishiguro, Kimiko; Tauchi, Kumi; Nomura, Ryuji.

In: Journal of Cell Biology, Vol. 152, No. 5, 05.03.2001, p. 1079-1085.

Research output: Contribution to journalArticle

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