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Traffic of prion protein between different compartments on the neuronal surface, and the propagation of prion disease
Author(s) -
Morris Roger J.,
Parkyn Celia J.,
Jen Angela
Publication year - 2006
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2006.07.053
Subject(s) - lipid raft , prion protein , microbiology and biotechnology , mechanism (biology) , cell , surface protein , chemistry , biology , biophysics , biochemistry , disease , virology , medicine , philosophy , epistemology , pathology
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.