Regulation of MHC Class I Assembly and Peptide Binding

  • Peaper D
  • Cresswell P
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Abstract

Peptide binding to {MHC} class I molecules is a component of a folding and assembly process that occurs in the endoplasmic reticulum {(ER)} and uses both cellular chaperones and dedicated factors. The involvement of glycoprotein quality-control chaperones and cellular oxidoreductases in peptide binding has led to models that are gradually being refined. Some aspects of the peptide loading process (e.g., the biosynthesis and degradation of {MHC} class I complexes) conform to models of glycoprotein quality control, but other aspects (e.g., the formation of a stable disulfide-linked dimer between tapasin and {ERp57)} deviate from models of chaperone and oxidoreductase function. Here we review what is known about the intersection of glycoprotein folding, oxidative reactions, and {MHC} class I peptide loading, emphasizing events that occur in the {ER} and within the {MHC} class I peptide loading complex.

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Authors

  • David R. Peaper

  • Peter Cresswell

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