Essential role of the prion protein N terminus in subcellular trafficking and half-life of cellular prion protein.

@article{Nunziante2003EssentialRO,
  title={Essential role of the prion protein N terminus in subcellular trafficking and half-life of cellular prion protein.},
  author={Max Nunziante and Sabine Gilch and Hermann M Sch{\"a}tzl},
  journal={The Journal of biological chemistry},
  year={2003},
  volume={278 6},
  pages={3726-34}
}
Aberrant metabolism and conformational alterations of the cellular prion protein (PrP(c)) are the underlying causes of transmissible spongiform encephalopathies in humans and animals. In cells, PrP(c) is modified post-translationally and transported along the secretory pathway to the plasma membrane, where it is attached to the cell surface by a glycosylphosphatidylinositol anchor. In surface biotinylation assays we observed that deletions within the unstructured N terminus of murine PrP(c) led… CONTINUE READING