期刊
BIOCHEMICAL SOCIETY TRANSACTIONS
卷 36, 期 -, 页码 1272-1276出版社
PORTLAND PRESS LTD
DOI: 10.1042/BST0361272
关键词
copper; endocytosis; lipid raft; low-density lipoprotein receptor-related protein-1 (LRP1); pnon; zinc
资金
- Medical Research Council
- Wellcome Trust
- MRC [G9824728] Funding Source: UKRI
- Medical Research Council [G9824728] Funding Source: researchfish
The cellular form of the prion protein, PrP(c), is critically required for the establishment of prion diseases, such as Creutzfeldt-jakob disease. Within the N-terminal half of PrP(c) are four octapeptide repeats that bind Cu(2+). Exposure of neuronal cells expressing PrP(c) to Cu(2+) results in the rapid endocytosis of the protein. First, PrPc translocates laterally out of detergent-resistant lipid rafts into detergent-soluble regions of the plasma membrane, then it is internalized through clathrin-coated pits. The extreme N-terminal region of PrP(c) is critically required for its endocytosis, as is the transmembrane LRP1 (low-density lipoprotein receptor-related protein-1). incubation of cells with a competitive inhibitor of LRP1 ligands, receptor-associated protein, or down-regulation of LRP1 with siRNA (short interfering RNA) reduces the endocytosis of PrPc. Zn(2+) also promotes the endocytosis of PrP(c), a phenomenon that is also dependent on the octapeptide repeats and requires LRP1.
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