The low-density lipoprotein receptor-related protein 1 (LRP1) mediates the endocytosis of the cellular prion protein

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 endocy...

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Bibliographic Details
Published in:Biochemical journal 2007-02, Vol.402 (1), p.17-23
Main Authors: Taylor, David R, Hooper, Nigel M
Format: Article
Language:English
Subjects:
Accelerated Publication
Amyloid beta-Protein Precursor - metabolism
Animals
Clathrin - metabolism
Copper - metabolism
Endocytosis
Humans
LDL-Receptor Related Protein-Associated Protein - metabolism
Ligands
Low Density Lipoprotein Receptor-Related Protein-1 - genetics
Low Density Lipoprotein Receptor-Related Protein-1 - metabolism
Mice
Microscopy, Fluorescence
Neuroblastoma - metabolism
Neurons - metabolism
PrPC Proteins - genetics
PrPC Proteins - metabolism
Receptors, LDL - genetics
Receptors, LDL - metabolism
RNA, Small Interfering - metabolism
Tumor Cells, Cultured
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Summary: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).
ISSN:0264-6021
1470-8728
DOI:10.1042/bj20061736