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- W2146209349 abstract "We recently identified an endoplasmic reticulum (ER) retrieval signal-the dilysine motif-in the glycoproteins of all five foamy viruses (FVs) for which sequences were available (P. A. Goepfert, G. Wang, and M. J. Mulligan, Cell 82:543-544, 1995). In the present study, expression of recombinant human FV (HFV) glycoprotein and analyses of oligosaccharide modifications and precursor cleavage indicated that the protein was localized to the ER. HFV glycoproteins encoding seven different dilysine motif mutations were then expressed. The results indicated that disruptions of the dilysine motif resulted in higher levels of forward transport of the HFV glycoprotein from the ER through the Golgi apparatus to the plasma membrane. We conclude that the dilysine motif is responsible for ER sorting of the FV glycoprotein. Signal-mediated ER localization has not previously been described for a retroviral glycoprotein." @default.
- W2146209349 created "2016-06-24" @default.
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- W2146209349 creator A5046912050 @default.
- W2146209349 creator A5064116200 @default.
- W2146209349 date "1997-01-01" @default.
- W2146209349 modified "2023-10-16" @default.
- W2146209349 title "A sorting motif localizes the foamy virus glycoprotein to the endoplasmic reticulum" @default.
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- W2146209349 doi "https://doi.org/10.1128/jvi.71.1.778-784.1997" @default.
- W2146209349 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/191117" @default.
- W2146209349 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/8985416" @default.
- W2146209349 hasPublicationYear "1997" @default.
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