Journal
FEBS LETTERS
Volume 580, Issue 23, Pages 5565-5571Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.febslet.2006.07.053
Keywords
amyloid; endocytosis; lipid domain; neuron; neurodegeneration; prion protein
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The key mechanism in prion disease is the conversion of cellular prion protein into an altered, pathogenic conformation, in which cellular mechanisms play a poorly understood role. Both forms of prion protein are lipid-anchored and reside in rafts that appear to protect the native conformation against conversion. Neurons rapidly traffic their cellular prion protein out of its lipid rafts to be endocytosed via coated pits before recycling back to the cell surface. it is argued in this review that understanding the mechanism of this trafficking holds the key to understanding the cellular role in the conformational conversion of prion protein. (c) 2006 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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