A glycolipid-anchored prion protein is endocytosed via clathrin-coated pits

@article{Shyng1994AGP,
  title={A glycolipid-anchored prion protein is endocytosed via clathrin-coated pits},
  author={Show-Ling Shyng and John E. Heuser and David A Harris},
  journal={The Journal of Cell Biology},
  year={1994},
  volume={125},
  pages={1239 - 1250}
}
The cellular prion protein (PrPc) is a glycolipid-anchored, cell surface protein of unknown function, a posttranslationally modified isoform of which PrPSc is involved in the pathogenesis of Creutzfeldt-Jakob disease, scrapie, and other spongiform encephalopathies. We have shown previously that chPrP, a chicken homologue of mammalian PrPC, constitutively cycles between the cell surface and an endocytic compartment, with a transit time of approximately 60 min in cultured neuroblastoma cells. We… CONTINUE READING