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• W2111315071 abstract "Yellow fever virus (YFV) encodes two envelope proteins, pre-membrane (prM) and envelope (E), that accumulate in the endoplasmic reticulum (ER). The C termini of prM and E form two antiparallel transmembrane alpha-helices that contain ER-retention signals. To understand further the ER retention of the prME heterodimer, we characterized the subcellular localization of chimeric proteins made of a reporter protein fused to the transmembrane segments of YFV envelope proteins. We showed that at least three of the transmembrane segments of the prME heterodimer are ER-retention signals. Interestingly, increasing the length of these alpha-helices led to the export of the chimeric proteins out of the ER. Furthermore, adding a diacidic export signal at the C terminus of the first transmembrane segment of the E protein also induced export to the cell surface. However, adding this export signal at the C terminus of the first transmembrane segment of E in the context of prME did not change the subcellular localization of the prME heterodimer, suggesting the presence of a stronger ER-retention signal outside the first transmembrane segment of E. Importantly, the diacidic export motif added to the C terminus of the first transmembrane segment of the prM protein was not sufficient to export a chimeric protein out of the ER, indicating that this sequence is a dominant ER-retention signal. Together, these data indicate that a combination of several signals of different strengths contributes to the ER retention of the YFV envelope protein heterodimer." @default.
• W2111315071 created "2016-06-24" @default.
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• W2111315071 date "2009-10-21" @default.
• W2111315071 modified "2023-10-18" @default.
• W2111315071 title "Identification of a dominant endoplasmic reticulum-retention signal in yellow fever virus pre-membrane protein" @default.
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• W2111315071 doi "https://doi.org/10.1099/vir.0.015339-0" @default.
• W2111315071 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/19846669" @default.
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