Abstract
PrP C (cellular prion protein) is located at the surface of neuronal cells in detergent-insoluble lipid rafts, yet is internalized by clathrin-dependent endocytosis. As PrP C is glycosyl- phosphatidylinositol-anchored, it requires a transmembrane adaptor protein to connect it to the clathrin endocytosis machinery. Using receptor-associated protein and small interfering RNA against particular LDL (low-density lipoprotein) family members, in combination with immunofluorescence microscopy and surface biotinylation assays, we show that the transmembrane LRP1 (LDL receptor-related protein 1) is required for the Cu 2+-mediated endocytosis of PrP C in neuronal cells. We show also that another LRP1 ligand that can cause neurodegenerative disease, the Alzheimer's amyloid precursor protein, does not modulate the endocytosis of PrP C. © 2007 Biochemical Society.
| Original language | English |
|---|---|
| Pages (from-to) | 17-23 |
| Number of pages | 6 |
| Journal | Biochemical Journal |
| Volume | 402 |
| Issue number | 1 |
| Publication status | Published - 15 Feb 2007 |
Keywords
- Amyloid precursor protein (APP)
- Clathrin
- Cu 2+-dependent endocytosis
- Low-density lipoprotein receptor-related protein-1 (LRP1)
- Prion
- Receptor-associated protein (RAP)
Research Beacons, Institutes and Platforms
- Dementia@Manchester