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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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Cholesterol Binding and Cholesterol Transport Proteins:

Part of the book series: Subcellular Biochemistry ((SCBI,volume 51))

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 which 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 the recent findings concerning the molecular architecture of the apical 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.

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Acknowledgements

We thank A. Hellwig for the excellent immunoelectron microscopy. D.C. was supported by the Deutsche Forschungsgemeinschaft (SFB/TR13-04 B1; SFB 655 A13/B3) and W.B.H. by the Deutsche Forschungsgemeinschaft (SPP 1111, Hu275/8-3; SFB/TR13-04 B1; SFB 655 A2).

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Corbeil, D., Marzesco, AM., 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: Harris, J. (eds) Cholesterol Binding and Cholesterol Transport Proteins:. Subcellular Biochemistry, vol 51. Springer, Dordrecht. https://doi.org/10.1007/978-90-481-8622-8_14

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