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Caveolin-2 Is Targeted to Lipid Droplets, a New “Membrane Domain” in the Cell

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Fujimoto, Toyoshi, Kogo, Hiroshi, Ishiguro, Kimiko, Tauchi, Kumi, Nomura, Ryuji·2001·The Journal of Cell Biology

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.

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Metadata

Authors
Fujimoto, T., Kogo, H., Ishiguro, K., Tauchi, K., & Nomura, R.
Venue
The Journal of Cell Biology
Published
2001-03-05
Volume
152
Issue
5
Pages
1079-1086
ISSN
  • 0021-9525 (ISSN-L)
  • 1540-8140
OpenAlex
W2147963733
Cited by
250
References
0
FWCI
7.32
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Caveolin-2 Is Targeted to Lipid Droplets, a New “Membrane Domain” in the Cell. https://app.cochat.ai/papers/10.1083/jcb.152.5.1079
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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. The Journal of Cell Biology. https://doi.org/10.1083/jcb.152.5.1079

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