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

Caveolin-1 and -2 constitute a framework of caveolae in nonmuscle cells. In the present study, we showed that caveolin-2, especially its beta isoform. Is targeted to the surface of lipid droplets (LD) by immunofluorescence an d 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 cent ral hydrophobic domain (residues 87-119) and the NH2-terminal (residues 70- 86) and COOH-terminal (residues 120-150) hydrophilic domains are ail necess ary 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 choleste rol 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.