Journal
JOURNAL OF IMMUNOLOGY
Volume 176, Issue 11, Pages 6464-6472Publisher
AMER ASSOC IMMUNOLOGISTS
DOI: 10.4049/jimmunol.176.11.6464
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Funding
- Medical Research Council [G0401569, G9800943, MC_U105178783] Funding Source: Medline
- Wellcome Trust Funding Source: Medline
- Medical Research Council [MC_U105178783, G9800943, G0401569] Funding Source: researchfish
- MRC [G0401569, MC_U105178783, G9800943] Funding Source: UKRI
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MHC class I molecules exit the endoplasmic reticulum (ER) by an unknown mechanism. Although a selective export mechanism has been proposed for the anterograde transport of class 1, a motif responsible for export has never been identified. Although classical class I molecules lacking their cytoplasmic tail are expressed on the cell surface, we found that HLA-F was entirely dependent on its cytoplasmic tail for export from the ER. Two known export motifs were recognizable in RLA-F. A C-terminal valine residue functioned in ER export and interacted with coat complex (COP)II, while an RxR motif also played an important role in anterograde transport and bound to 14-3-3 proteins. This divergent trafficking of HLA-F implicates an alternative function for HLA-F, independent of loading with peptides in the ER.
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