Article
Post-translational import of the prion protein into the endoplasmic reticulum interferes with cell viability: a critical role for the putative transmembrane domain.
The Journal of biological chemistry - 19 Sept 2003
Heller Ulrich, Winklhofer Konstanze F, Heske Johanna, Reintjes Anja, Tatzelt Jörg
Abstract excerpt
Aberrant folding of the mammalian prion protein (PrP) is linked to prion diseases in humans and animals. We show that during post-translational targeting of PrP to the endoplasmic reticulum (ER) the putative transmembrane domain induces misfolding of PrP in the cytosol and interferes with its import into the ER. Unglycosylated and misfolded PrP with an uncleaved N-terminal signal sequence associates with ER...
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