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  • Title: The double role of the endoplasmic reticulum chaperone tapasin in peptide optimization of HLA class I molecules.
    Author: Cabrera CM.
    Journal: Scand J Immunol; 2007 Jun; 65(6):487-93. PubMed ID: 17523940.
    Abstract:
    During the assembly of the HLA class I molecules with peptides in the peptide-loading complex, a series of transient interactions are made with ER-resident chaperones. These interactions culminate in the trafficking of the HLA class I molecules to the cell surface and presentation of peptides to CD8(+) T lymphocytes. Within the peptide-loading complex, the glycoprotein tapasin exhibits a relevant function. This immunoglobulin (Ig) superfamily member in the endoplasmic reticulum membrane tethers empty HLA class I molecules to the transporter associated with antigen-processing (TAP) proteins. This review will address the current concepts regarding the double role that tapasin plays in the peptide optimization and surface expression of the HLA class I molecules.
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