IMR Press / FBL / Volume 16 / Issue 1 / DOI: 10.2741/3681

Frontiers in Bioscience-Landmark (FBL) is published by IMR Press from Volume 26 Issue 5 (2021). Previous articles were published by another publisher on a subscription basis, and they are hosted by IMR Press on as a courtesy and upon agreement with Frontiers in Bioscience.

Open Access Article
The role of lipid rafts in prion protein biology
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1 Department of Pathology, University of Melbourne, Victoria 3010, Australia
2 Institute of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds LS2 9JT, UK
Academic Editor:Sophie Mouillet-Richard
Front. Biosci. (Landmark Ed) 2011, 16(1), 151–168;
Published: 1 January 2011
(This article belongs to the Special Issue Cellular prion protein partners and signaling)

The conformational conversion of the cellular prion protein, PrP(C), to the misfolded isoform PrP(Sc )is the central pathogenic event in the uniquely transmissible neurodegenerative prion diseases. As both PrP(C) and PrP(Sc) are associated with membranes, the nature of the membrane microenvironment may well play a significant role in both the conformational conversion process as well as the normal functions of PrP(C). Within the membrane are various microdomains, areas of distinct lipid and protein composition, the best studied of which are the cholesterol- and sphingolipid-rich lipid rafts. These domains are characterized biochemically by their relative resistance to solubilization in certain detergents at low temperature. In this article we review the evidence for the involvement of lipid rafts in the localization and trafficking of PrP(C), in the cellular signaling, neuroprotective and metal binding functions of PrP(C), and as sites for the conversion of PrP(C) to PrP(Sc) and in cell-to-cell prion transmission.

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