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Selective Export of HLA-F by Its Cytoplasmic Tail¹

Louise H. Boyle^2,3,*, Alison K. Gillingham^3,, Sean Munro and John Trowsdale^*

^* Department of Pathology, University of Cambridge, Cambridge, United Kingdom; and Medical Research Council Laboratory of Molecular Biology, Cambridge, United Kingdom

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 I, 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 HLA-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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