Prion protein-related proteins from zebrafish are complex glycosylated and contain a glycosylphosphatidylinositol anchor.
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.
Miesbauer
Margit
M
Max-Planck-Institute for Biochemistry, Martinsried, Germany.
Bamme
Theresa
T
Riemer
Constanze
C
Oidtmann
Birgit
B
Winklhofer
Konstanze F
KF
Baier
Michael
M
Tatzelt
Jörg
J
D000595:Amino Acid Sequence; D000818:Animals; D004721:Endoplasmic Reticulum / Q000378:metabolism*; D006031:Glycosylation; D017261:Glycosylphosphatidylinositols / Q000737:chemistry* / Q000378:metabolism*; D051379:Mice; D008969:Molecular Sequence Data; D011328:Prions / Q000737:chemistry* / Q000378:metabolism*; D015027:Zebrafish / Q000378:metabolism*
D017261:Glycosylphosphatidylinositols; D011328:Prions