Scrapie-like prion protein is translocated to the nuclei of infected cells independently of proteasome inhibition and interacts with chromatin.

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 Sci

journal_title

Journal of cell science

authors

Mangé A,Crozet C,Lehmann S,Béranger F

doi

10.1242/jcs.01094

keywords:

subject

Has Abstract

pub_date

2004-05-01 00:00:00

pages

2411-6

issue

Pt 11

eissn

0021-9533

issn

1477-9137

pii

117/11/2411

journal_volume

117

pub_type

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