Article abstract
Nature Immunology 8, 864 - 872 (2007)
Published online: 1 July 2007 | doi:10.1038/ni1483
Redox regulation of peptide receptivity of major histocompatibility complex class I molecules by ERp57 and tapasin
Alexandra Kienast1, Marc Preuss1, Monique Winkler1 & Tobias P Dick1
Abstract
The function of the oxidoreductase ERp57 in the major histocompatibility complex (MHC) class I peptide-loading complex has remained elusive. Here we show that in the absence of tapasin, the 
2 disulfide bond in the MHC class I peptide-binding groove was rapidly reduced. Covalent sequestration of ERp57 by tapasin was needed to protect the 2 disulfide bond against reduction and thus to maintain the binding groove in a peptide-receptive state. Allelic variations in MHC class I tapasin dependency reflected their susceptibility to reduction of the 2 disulfide bond. In the absence of sequestration, ERp57 acted directly on the 2 disulfide bond. Our work provides insight into how the immune system customizes 'quality control' in the endoplasmic reticulum to fit the needs of antigen presentation.
- Redox Regulation Research Group, German Cancer Research Center, D-69120 Heidelberg, Germany.
Correspondence to: Tobias P Dick1 e-mail: t.dick@dkfz.de
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