Prion diseases are fatal neurodegenerative disorders that include Creutzfeldt–Jakob disease in humans and bovine spongiform encephalopathy in animals. They are unique in terms of their biology because they are caused by the conformational re-arrangement of a normal host-encoded prion protein, PrP C , to an abnormal infectious isoform, PrP Sc . Currently the precise mechanism behind prion-mediated neurodegeneration remains unclear. It is hypothesised than an unknown toxic gain of function of PrP Sc , or an intermediate oligomeric form, underlies neuronal death. Increasing evidence suggests a role for the ubiquitin proteasome system (UPS) in prion disease. Both wild-type PrP C and disease-associated PrP isoforms accumulate in cells after proteasome inhibition leading to increased cell death, and abnormal β-sheet-rich PrP isoforms have been shown to inhibit the catalytic activity of the proteasome. Here we review potential interactions between prions and the proteasome outlining how the UPS may be implicated in prion-mediated neurodegeneration.
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Prions and the proteasome
Deriziotis, Pelagia; Tabrizi, Sarah J.
Follow Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease
, Volume 1782 (12)
Elsevier – Dec 1, 2008
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