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A more recent version of this article appeared on September 26, 2003
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Papers In Press, published online ahead of print July 14, 2003
J. Biol. Chem, 10.1074/jbc.M302036200
Submitted on February 26, 2003
Revised on July 14, 2003
Accepted on July 14, 2003

The N-terminal region of the prion protein ectodomain contains a lipid raft targeting determinant

Adrian R. Walmsley, Fanning Zeng, and Nigel M. Hooper

School of Biochemistry and Molecular Biology, University of Leeds, Leeds, W. Yorks. LS2 9JT

Corresponding Author: n.m.hooper{at}leeds.ac.uk

The association of the prion protein (PrP) with sphingolipid- and cholesterol-rich lipid rafts is instrumental in the pathogenesis of the neurodegenerative prion diseases. Although the glycosyl-phosphatidylinositol (GPI) anchor is an exoplasmic determinant of raft association, PrP remained raft associated in human neuronal cells even when the GPI anchor was deleted or substituted for a transmembrane anchor indicating that the ectodomain contains a raft localisation signal. The raft association of transmembrane-anchored PrP occurred independently of Cu(II) binding as it failed to be abolished by either deletion of the octapeptide repeat region (residues 51-90) or treatment of cells with a Cu(II) chelator. Raft association of transmembrane-anchored PrP was only abolished by the deletion of the N-terminal region (residues 23-90) of the ectodomain. This region was sufficient to confer raft localisation when fused to the N-terminus of a non-raft transmembrane-anchored protein and suppressed the clathrin-coated pit localisation signal in the cytoplasmic domain of the amyloid precursor protein. These data indicate that the N-terminal region of PrP acts as a cellular raft targeting determinant and that residues 23-90 of PrP represent the first proteinaceous raft targeting signal within the ectodomain of a GPI anchored protein.


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