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Assembly of MHC class I molecules within the endoplasmic reticulum

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Abstract

MHC class I molecules bind cytosolically derived peptides within the endoplasmic reticulum (ER) and present them at the cell surface to cytotoxic T cells. A major focus of our laboratory has been to understand the functions of the diverse proteins involved in the intracellular assembly of MHC class I molecules. These include the molecular chaperones calnexin and calreticulin, which enhance the proper folding and subunit assembly of class I molecules and also retain assembly intermediates within the ER; ERp57, a thiol oxidoreductase that promotes heavy chain disulfide formation and proper assembly of the peptide loading complex; tapasin which recruits class I molecules to the TAP peptide transporter and enhances the loading of high affinity peptide ligands; and Bap31, which is involved in clustering assembled class I molecules at ER exit sites for export along the secretory pathway. This review describes our contributions to elucidating the functions of these proteins; the combined effort of many dedicated students and post-doctoral fellows.

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Authors and Affiliations

  1. Department of and Immunology, University of Toronto, Toronto, Ontario, Canada

    Yinan Zhang &  David B. Williams

  2. Department of Biochemistry, University of Toronto, Medical Sciences Bldg., M5S 1A8, Toronto, Ontario, Canada

    Yinan Zhang &  David B. Williams

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  1. Yinan Zhang
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Correspondence to David B. Williams.

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Zhang, Y., Williams, D.B. Assembly of MHC class I molecules within the endoplasmic reticulum. Immunol Res 35, 151–162 (2006). https://doi.org/10.1385/IR:35:1:151

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