Journal
BIOLOGICAL CHEMISTRY
Volume 385, Issue 9, Pages 763-778Publisher
WALTER DE GRUYTER GMBH
DOI: 10.1515/BC.2004.100
Keywords
calreticulin; ERp57; major histocompatibility complex molecules; peptide binding; TAP; tapasin
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MHC (major histocompatibility complex) class I molecules bind intracellular virusderived peptides in the endoplasmic reticulum (ER) and present them at the cell surface to cytotoxic T lymphocytes. Peptidefree class I molecules at the cell surface, however, could lead to aberrant T cell killing. Therefore, cells ensure that class I molecules bind highaffinity ligand peptides in the ER, and restrict the export of empty class I molecules to the Golgi apparatus. For both of these safeguard mechanisms, the MHC class I loading complex (which consists of the peptide transporter TAP, the chaperones tapasin and calreticulin, and the protein disulfide isomerase ERp57) plays a central role. This article reviews the actions of accessory proteins in the biogenesis of class I molecules, specifically the functions of the loading complex in highaffinity peptide binding and localization of class I molecules, and the known connections between these two regulatory mechanisms. It introduces new models for the mode of action of tapasin, the role of the class I loading complex in peptide editing, and the intracellular localization of class I molecules.
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