The role of rafts in the fibrillization and aggregation of prions.
A key molecular event in prion diseases is the conversion of the prion protein (PrP) from its normal cellular form (PrP(C)) to the disease-specific form (PrP(Sc)). The transition from PrP(C) to PrP(Sc) involves a major conformational change, resulting in amorphous aggregates and/or fibrillar amyloid deposits. Here several lines of evidence implicating membranes in the conversion of PrP are reviewed with a particular emphasis on the role of lipid rafts in the conformational transition of prion proteins. New correlations between in vitro biophysical studies and findings from cell biology work on the role of rafts in prion conversion are highlighted and a mechanism for the role of rafts in prion conversion is proposed.
Pinheiro
Teresa J T
TJ
Department of Biological Sciences, University of Warwick, Coventry, UK. t.pinheiro@warwick.ac.uk
D000818:Animals; D002462:Cell Membrane / Q000378:metabolism; D004705:Endocytosis; D006056:Golgi Apparatus / Q000378:metabolism; D006801:Humans; D008563:Membrane Lipids / Q000737:chemistry* / Q000378:metabolism; D021962:Membrane Microdomains / Q000737:chemistry / Q000378:metabolism; D008968:Molecular Conformation; D018621:PrPC Proteins / Q000737:chemistry* / Q000378:metabolism; D018620:PrPSc Proteins / Q000737:chemistry* / Q000378:metabolism; D017096:Prion Diseases / Q000209:etiology / Q000378:metabolism; D011328:Prions / Q000737:chemistry* / Q000378:metabolism; D017510:Protein Folding
D008563:Membrane Lipids; D018621:PrPC Proteins; D018620:PrPSc Proteins; D011328:Prions