Selective export of HLA-F by its cytoplasmic tail.

Article Details

Citation

Boyle LH, Gillingham AK, Munro S, Trowsdale J

Selective export of HLA-F by its cytoplasmic tail.

J Immunol. 2006 Jun 1;176(11):6464-72. doi: 10.4049/jimmunol.176.11.6464.

PubMed ID
16709803 [ View in PubMed
]
Abstract

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.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
HLA class I histocompatibility antigen, alpha chain FP30511Details