Prion protein-related proteins from zebrafish are complex glycosylated and contain a glycosylphosphatidylinositol anchor |
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Authors: | Miesbauer Margit Bamme Theresa Riemer Constanze Oidtmann Birgit Winklhofer Konstanze F Baier Michael Tatzelt Jörg |
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Affiliation: | Max-Planck-Institute for Biochemistry, Martinsried, Germany. |
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Abstract: | A hallmark of prion diseases in mammals is a conformational transition of the cellular prion protein (PrP(C)) into a pathogenic isoform termed PrP(Sc). PrP(C) is highly conserved in mammals, moreover, genes of PrP-related proteins have been recently identified in fish. While there is only little sequence homology to mammalian PrP, PrP-related fish proteins were predicted to be modified with N-linked glycans and a C-terminal glycosylphosphatidylinositol (GPI) anchor. We biochemically characterized two PrP-related proteins from zebrafish in cultured cells and show that both zePrP1 and zeSho2 are imported into the endoplasmic reticulum and are post-translationally modified with complex glycans and a C-terminal GPI anchor. |
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Keywords: | Prion Scrapie GPI anchor Zebrafish Sho |
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