VIP21/caveolin is a cholesterol-binding protein.

Abstract

VIP21/caveolin is localized to both caveolae and apical transport vesicles and presumably cycles between the cell surface and the Golgi complex. We have studied the lipid interactions of this protein by reconstituting Escherichia coli-expressed VIP21/caveolin into liposomes. Surprisingly, the protein reconstituted only with cholesterol-containing lipid mixtures. We demonstrated that the protein binds at least 1 mol of cholesterol per mole of protein and that this binding promotes formation of protein oligomers. These findings suggest that VIP21/caveolin, through its cholesterol-binding properties, serves a specific function in microdomain formation during membrane trafficking.

Keywords

CaveolaeGolgi apparatusVesicleLipid microdomainCholesterolLiposomeBiochemistryLipid raftCell biologyCaveolin 1Binding proteinChemistryMembrane proteinPlasma protein bindingBiologyMembraneCell

Affiliated Institutions

European Molecular Biology Laboratory DE

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Publication Info

Year: 1995
Type: article
Volume: 92
Issue: 22
Pages: 10339-10343
Citations: 884
Access: Closed

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APA Style

                            
                                
                                    Masayuki Murata, 
                                
                                    Johan Peränen, 
                                
                                    Rupert Schreiner
                                
                                et al.
                            
                            (1995). 
                            VIP21/caveolin is a cholesterol-binding protein.. 
                            Proceedings of the National Academy of Sciences
                            , 92
                            (22)
                            , 10339-10343.
                            https://doi.org/10.1073/pnas.92.22.10339
                        

Identifiers

DOI: 10.1073/pnas.92.22.10339