spacer gif spacer gif spacer gif spacer gif spacer gif
QUICK SEARCH:   [advanced]


spacer gif
     Home     Help     Feedback     Subscriptions     Archive     Search     Table of Contents    

First published online May 4, 2004
doi: 10.1242/10.1242/jcs.01094

Journal of Cell Science 117, 2411-2416 (2004)
Published by The Company of Biologists 2004
This Article
Right arrow Figures Only
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Mangé, A.
Right arrow Articles by Béranger, F.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Mangé, A.
Right arrow Articles by Béranger, F.

Research Article

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

Alain Mangé*, Carole Crozet*, Sylvain Lehmann and Florence Béranger{ddagger}

Institut de Génétique Humaine, UPR CNRS1142, 141 Rue de la Cardonille 34396 Montpellier CEDEX 5, France

{ddagger} Author for correspondence (e-mail: florence.beranger{at}igh.cnrs.fr)

Accepted 9 January 2004

Prion diseases are fatal transmissible neurodegenerative disorders characterized by the accumulation of an abnormally folded isoform of the cellular prion protein (PrPC) denoted PrPSc. 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

Key words: Prion, Nucleus, Microtubules




This article has been cited by other articles:


Home page
 J. Biol. Chem.Home page
X. Wang, F. Wang, L. Arterburn, R. Wollmann, and J. Ma
The Interaction between Cytoplasmic Prion Protein and the Hydrophobic Lipid Core of Membrane Correlates with Neurotoxicity
J. Biol. Chem., May 12, 2006; 281(19): 13559 - 13565.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Cell. Biol.Home page
Y. Gu, X. Luo, S. Basu, H. Fujioka, and N. Singh
Cell-specific metabolism and pathogenesis of transmembrane prion protein.
Mol. Cell. Biol., April 1, 2006; 26(7): 2697 - 2715.
[Abstract] [Full Text] [PDF]

Home page
 J. Cell Sci.Home page
C. Crozet, Y.-L. Lin, C. Mettling, C. Mourton-Gilles, P. Corbeau, S. Lehmann, and V. Perrier
Inhibition of PrPSc formation by lentiviral gene transfer of PrP containing dominant negative mutations
J. Cell Sci., November 1, 2004; 117(23): 5591 - 5597.
[Abstract] [Full Text] [PDF]


© The Company of Biologists Ltd 2004