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Antigen presentation

Maintaining the groove

Nature Reviews Immunology volume 7, pages 582–583 (2007)Cite this article

...functions previously proposed for tapasin alone are instead properties of the tapasin–ERp57 heterodimer.

Wearsch and Cresswell had previously had little success in their attempts to reconstitute functional interactions between monomeric tapasin and heavy-chain–β2m heterodimers, so they established a cell-free in vitro system to reconstitute the structural and functional interactions of a PLC without TAP (termed the subcomplex). They combined cell extracts from tapasin-deficient cells that contained components of the PLC with either recombinant soluble tapasin or tapasin–ERp57 conjugates, and assessed the complexes that were formed. Only the tapasin–ERp57 conjugates, and not the monomeric tapasin, were able to mediate subcomplex formation, stabilize empty peptide-receptive heavy-chain–β2m heterodimers and facilitate peptide loading. They reasoned that if tapasin–ERp57 conjugates also acted as peptide editors for preferential binding of high-affinity peptides to MHC class I molecules, then the presence of the conjugates should allow binding of more high-affinity peptides; and this was indeed the case. So, the functions previously proposed for tapasin alone are instead properties of the tapasin–ERp57 heterodimer.

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ORIGINAL RESEARCH PAPERS

  1. Wearsch, P. A. & Cresswell, P. Selective loading of high-affinity peptides onto major histocompatibility complex class I molecules by the tapasin-ERp57 heterodimer. Nature Immunol. 1 July 2007 (doi:10.1038/ni1485)

  2. Kienast, A., Preuss, M., Winkler, M., Dick, T. P. Redox regulation of peptide receptivity of major histocompatibility complex class I molecules by ERp57 and tapasin. Nature Immunol. 1 July 2007 (doi:10.1038/ni1483)

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  1. Elaine Bell
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Bell, E. Maintaining the groove. Nat Rev Immunol 7, 582–583 (2007). https://doi.org/10.1038/nri2140

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  • DOI: https://doi.org/10.1038/nri2140

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