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Trafficking of prion proteins through a caveolae-mediated endosomal pathway

Academic Article
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Overview

authors

  • Peters, P. J.
  • Mironov, A.
  • Peretz, D.
  • van Donselaar, E.
  • Leclerc, E.
  • Erpel, S.
  • DeArmond, S. J.
  • Burton, Dennis
  • Williamson, R. A.
  • Vey, M.
  • Prusiner, S. B.

publication date

  • August 2003

journal

  • Journal of Cell Biology  Journal

abstract

  • To understand the posttranslational conversion of the cellular prion protein (PrPC) to its pathologic conformation, it is important to define the intracellular trafficking pathway of PrPC within the endomembrane system. We studied the localization and internalization of PrPC in CHO cells using cryoimmunogold electron microscopy. At steady state, PrPC was enriched in caveolae both at the TGN and plasma membrane and in interconnecting chains of endocytic caveolae. Protein A-gold particles bound specifically to PrPC on live cells. These complexes were delivered via caveolae to the pericentriolar region and via nonclassical, caveolae-containing early endocytic structures to late endosomes/lysosomes, thereby bypassing the internalization pathway mediated by clathrin-coated vesicles. Endocytosed PrPC-containing caveolae were not directed to the ER and Golgi complex. Uptake of caveolae and degradation of PrPC was slow and sensitive to filipin. This caveolae-dependent endocytic pathway was not observed for several other glycosylphosphatidyl inositol (GPI)-anchored proteins. We propose that this nonclassical endocytic pathway is likely to determine the subcellular location of PrPC conversion.

subject areas

  • Animals
  • Bacterial Proteins
  • CHO Cells
  • Caveolae
  • Caveolin 1
  • Caveolins
  • Cricetinae
  • Endosomes
  • Gold Colloid
  • Microscopy, Electron
  • Prions
  • Protein Transport
  • Receptors, Transferrin
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Research

keywords

  • caveolae
  • cryoimmunogold
  • electron microscopy
  • endosomal pathway
  • prion
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Identity

PubMed Central ID

  • PMC2173792

International Standard Serial Number (ISSN)

  • 0021-9525

Digital Object Identifier (DOI)

  • 10.1083/jcb.200304140

PubMed ID

  • 12925711
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Additional Document Info

start page

  • 703

end page

  • 717

volume

  • 162

issue

  • 4

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