A sorting motif localizes the foamy virus glycoprotein to the endoplasmic reticulum.
AUTOR(ES)
Goepfert, P A
RESUMO
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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=191117Documentos Relacionados
- Translocation of rubella virus glycoprotein E1 into the endoplasmic reticulum.
- How N-linked oligosaccharides affect glycoprotein folding in the endoplasmic reticulum.
- Identification of a consensus motif for retention of transmembrane proteins in the endoplasmic reticulum.
- Dissociation and reassociation of oligomeric viral glycoprotein subunits in the endoplasmic reticulum.
- The rotavirus nonstructural glycoprotein NSP4 mobilizes Ca2+ from the endoplasmic reticulum.
