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

Caveolin-2 is targeted to lipid droplets, a new "membrane domain" in the cell.
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DOI:
10.1083/jcb.152.5.1079
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发表时间:
2001-03-05
期刊:
The Journal of cell biology
影响因子:
--
通讯作者:
Nomura R
Nomura R
中科院分区:
其他
文献类型:
--
作者:
Fujimoto T;Kogo H;Ishiguro K;Tauchi K;Nomura R

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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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