TAPBPR alters MHC class I peptide presentation by functioning as a peptide exchange catalyst
Hermann, Clemens, Van Hateren, Andy, Trautwein, Nico, Neerincx, Andreas, Duriez, Patrick J., Stevanović, Stefan, Trowsdale, John, Deane, Janet E., Elliott, Tim and Boyle, Louise H. (2015) TAPBPR alters MHC class I peptide presentation by functioning as a peptide exchange catalyst eLife, 4, (e09617), pp. 1-22. (doi:10.7554/eLife.09617.001). (PMID:26439010).
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Our understanding of the antigen presentation pathway has recently been enhanced with the identification that the tapasin-related protein TAPBPR is a second MHC I-specific chaperone. We sought to determine whether, like tapasin, TAPBPR can also influence MHC I peptide selection by functioning as a peptide exchange catalyst. We show that TAPBPR can catalyse the dissociation of peptides from peptide-MHC I complexes, enhance the loading of peptide-receptive MHC I molecules, and discriminate between peptides based on affinity in vitro. In cells, the depletion of TAPBPR increased the diversity of peptides presented on MHC I molecules, suggesting that TAPBPR is involved in restricting peptide presentation. Our results suggest TAPBPR binds to MHC I in a peptide-receptive state and, like tapasin, works to enhance peptide optimisation. It is now clear there are two MHC class I specific peptide editors, tapasin and TAPBPR, intimately involved in controlling peptide presentation to the immune system.
|Digital Object Identifier (DOI):||doi:10.7554/eLife.09617.001|
|Subjects:||R Medicine > RC Internal medicine > RC0254 Neoplasms. Tumors. Oncology (including Cancer)|
|Organisations:||Southampton Cancer Research UK Centre, Cancer Sciences|
|Date Deposited:||15 Dec 2015 14:44|
|Last Modified:||22 Feb 2017 07:14|
|Further Information:||Google Scholar|
|RDF:||RDF+N-Triples, RDF+N3, RDF+XML, Browse.|
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