Abstract:
:Prion diseases are fatal transmissible neurodegenerative disorders characterized by the accumulation of an abnormally folded isoform of the cellular prion protein (PrP(C)) denoted PrP(Sc). Recently, wild-type and pathogenic PrP mutants have been shown to be degraded by the endoplasmic reticulum-associated degradation proteasome pathway after translocation into the cytosol. We show here that a protease resistant form of PrP accumulated in the nuclei of prion-infected cells independently of proteasome activity, and that this nuclear translocation required an intact microtubule network. Moreover, our results show for the first time that nuclear PrP interacts with chromatin in vivo, which may have physiopathological consequences in prion diseases
journal_name
J Cell Scijournal_title
Journal of cell scienceauthors
Mangé A,Crozet C,Lehmann S,Béranger Fdoi
10.1242/jcs.01094keywords:
subject
Has Abstractpub_date
2004-05-01 00:00:00pages
2411-6issue
Pt 11eissn
0021-9533issn
1477-9137pii
117/11/2411journal_volume
117pub_type
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