Traffic of prion protein between different compartments on the neuronal surface, and the propagation of prion disease |
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Authors: | Morris Roger J Parkyn Celia J Jen Angela |
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Institution: | Wolfson Centre for Age-Related Diseases, Guy's Hospital Campus, King's College, London SE1 1UL, United Kingdom. roger.morris@kcl.ac.uk |
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Abstract: | 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. |
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Keywords: | Amyloid Endocytosis Lipid domain Neuron Neurodegeneration Prion protein |
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