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Prominin-1: a distinct cholesterol-binding membrane protein and the organisation of the apical plasma membrane of epithelial cells

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Corbeil,  Denis
Max Planck Institute of Molecular Cell Biology and Genetics, Max Planck Society;

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Marzesco,  Anne-Marie
Max Planck Institute of Molecular Cell Biology and Genetics, Max Planck Society;

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Fargeas,  Christine A.
Max Planck Institute of Molecular Cell Biology and Genetics, Max Planck Society;

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Huttner,  Wieland B.
Max Planck Institute of Molecular Cell Biology and Genetics, Max Planck Society;

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Citation

Corbeil, D., Marzesco, A.-M., Fargeas, C. A., & Huttner, W. B. (2010). Prominin-1: a distinct cholesterol-binding membrane protein and the organisation of the apical plasma membrane of epithelial cells. In J. R. Harris (Ed.), Cholesterol binding and cholesterol transport proteins: structure and function in health and disease (pp. 399-423). Dordrecht: Springer.


Cite as: https://hdl.handle.net/21.11116/0000-0001-0BFB-9
Abstract
The apical plasma membrane of polarized epithelial cells is composed of distinct subdomains, that is, planar regions and protrusions (microvilli, primary cilium), each of wich are constructed from specific membrane microdomains. Assemblies containing the pentaspan glycoprotein prominin-1 and certain membrane lipids, notably cholesterol, are characteristic features of these microdomains in apical membrane protrusions. Here we highlight teh recent findings concerning the molecular architecture of the aipical plasma membrane of epithelial cells and its dynamics. The latter is illustrated by the budding and fission of prominin-1-containing membrane vesicles from apical plasma membrane protrusions, which is controlled, at least in part, by the level of membrane cholesterol and the cholesterol-dependent organization of membrane microdomains.