Réticulum endoplasmique, protéasome et maladies à prions

Florence Béranger; Alain Mangé; Sylvain Lehmann

doi:10.1051/medsci/20031989778

Accès gratuit

Numéro		Med Sci (Paris) Volume 19, Numéro 8-9, Août-Septembre 2003


Page(s)		778 - 780
Section		Le Magazine : Nouvelles
DOI		https://doi.org/10.1051/medsci/20031989778
Publié en ligne		15 août 2003

Collinge J. Prion diseases of humans and animals: their causes and molecular basis. Annu Rev Neurosci 2001; 24: 519–50. [Google Scholar]
Zerial M, McBride H. Rab proteins as membrane organizers. Nat Rev Mol Cell Biol 2001; 2: 107–17. [Google Scholar]
Beranger F, Mange A, Goud B, Lehmann S. Stimulation of PrP(C) retrograde transport toward the endoplasmic reticulum increases accumulation of PrP(Sc) in prion-infected cells. J Biol Chem 2002; 277: 38972–7. [Google Scholar]
Yedidia Y, Horonchik L, Tzaban S, Yanai A, Taraboulos A. Proteasomes and ubiquitin are involved in the turnover of the wildtype prion protein. EMBO J 2001; 20: 5383–91. [Google Scholar]
Ma J, Lindquist S. Wild-type PrP and a mutant associated with prion disease are subject to retrograde transport and proteasome degradation. Proc Natl Acad Sci USA 2001; 98: 14955–60. [Google Scholar]
Ma J, Lindquist S. Conversion of PrP to a selfperpetuating PrPSc-like conformation in the cytosol. Science 2002; 298: 1785–8. [Google Scholar]
Ma J, Wollmann R, Lindquist S. Neurotoxicity and neurodegeneration when PrP accumulates in the cytosol. Science 2002; 298: 1781–5. [Google Scholar]
Cohen E, Taraboulos A. Scrapie-like prion protein accumulates in aggresomes of cyclosporin A-treated cells. EMBO J 2003; 22: 404–17. [Google Scholar]

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[1] Collinge J. Prion diseases of humans and animals: their causes and molecular basis. Annu Rev Neurosci 2001; 24: 519–50. [Google Scholar]

[2] Zerial M, McBride H. Rab proteins as membrane organizers. Nat Rev Mol Cell Biol 2001; 2: 107–17. [Google Scholar]

[3] Beranger F, Mange A, Goud B, Lehmann S. Stimulation of PrP(C) retrograde transport toward the endoplasmic reticulum increases accumulation of PrP(Sc) in prion-infected cells. J Biol Chem 2002; 277: 38972–7. [Google Scholar]

[4] Yedidia Y, Horonchik L, Tzaban S, Yanai A, Taraboulos A. Proteasomes and ubiquitin are involved in the turnover of the wildtype prion protein. EMBO J 2001; 20: 5383–91. [Google Scholar]

[5] Ma J, Lindquist S. Wild-type PrP and a mutant associated with prion disease are subject to retrograde transport and proteasome degradation. Proc Natl Acad Sci USA 2001; 98: 14955–60. [Google Scholar]

[6] Ma J, Lindquist S. Conversion of PrP to a selfperpetuating PrPSc-like conformation in the cytosol. Science 2002; 298: 1785–8. [Google Scholar]

[7] Ma J, Wollmann R, Lindquist S. Neurotoxicity and neurodegeneration when PrP accumulates in the cytosol. Science 2002; 298: 1781–5. [Google Scholar]

[8] Cohen E, Taraboulos A. Scrapie-like prion protein accumulates in aggresomes of cyclosporin A-treated cells. EMBO J 2003; 22: 404–17. [Google Scholar]