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VIP21/caveolin is a cholesterol-binding protein

Item Type:Article
Title:VIP21/caveolin is a cholesterol-binding protein
Creators Name:Murata, M. and Peraenen, J. and Schreiner, R. and Wieland, F. and Kurzchalia, T.V. and Simons, K.
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:Base Sequence, Carrier Proteins, Caveolin 1, Caveolins, Cholesterol, DNA Primers, Escherichia Coli, Histidine, Kinetics, Liposomes, Lung, Membrane Proteins, Molecular Sequence Data, Phospholipids, Polymerase Chain Reaction, Recombinant Proteins, Sequence Tagged Sites, Structure-Activity Relationship, Animals, Dogs
Source:Proceedings of the National Academy of Sciences of the United States of America
Publisher:National Academy of Sciences
Page Range:10339-10343
Date:24 October 1995
Official Publication:http://www.ncbi.nlm.nih.gov/pmc/articles/PMC40792/?tool=pubmed
PubMed:View item in PubMed

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