Caveolin, a protein component of caveolae membrane coats.

Abstract

Caveolae have been implicated in the transcytosis of macromolecules across endothelial cells and in the receptor-mediated uptake of 5-methyltetrahydrofolate. Structural studies indicate that caveolae are decorated on their cytoplasmic surface by a unique array of filaments or strands that form striated coatings. To understand how these nonclathrin-coated pits function, we performed structural analysis of the striated coat and searched for the molecular component(s) of the coat material. The coat cannot be removed by washing with high salt; however, exposure of membranes to cholesterol-binding drugs caused invaginated caveolae to flatten and the striated coat to disassemble. Antibodies directed against a 22 kd substrate for v-src tyrosine kinase in virus-transformed chick embryo fibroblasts decorated the filaments, suggesting that this molecule is a component of the coat. We have named the molecule caveolin. Caveolae represent a third type of coated membrane specialization that is involved in molecular transport.

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@article{Rothberg1992CaveolinAP, title={Caveolin, a protein component of caveolae membrane coats.}, author={Karen G. Rothberg and John E. Heuser and W C Donzell and Yanting Ying and J R Glenney and Richard G.W Anderson}, journal={Cell}, year={1992}, volume={68 4}, pages={673-82} }