期刊
MOLECULAR BIOLOGY OF THE CELL
卷 12, 期 4, 页码 881-889出版社
AMER SOC CELL BIOLOGY
DOI: 10.1091/mbc.12.4.881
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- NINDS NIH HHS [T32-NS07129, NS35496, T32 NS007129] Funding Source: Medline
Although there is considerable evidence that PrPSc is the infectious form of the prion protein, it has recently been proposed that a transmembrane variant called (PrP)-Pr-Ctm is the direct cause of prion-associated neurodegeneration. We report here, using a mutant form of PrP that is synthesized exclusively with the (PrP)-Pr-Ctm topology, that (PrP)-Pr-Ctm is retained in the endoplasmic reticulum and is degraded by the proteasome. We also demonstrate that (PrP)-Pr-Ctm contains an uncleaved, N-terminal signal peptide as well as a C-terminal glycolipid anchor. These results provide insight into general mechanisms that control the topology of membrane proteins during their synthesis in the endoplasmic reticulum, and they also suggest possible cellular pathways by which (PrP)-Pr-Ctm may cause disease.
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