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The double role of the endoplasmic reticulum chaperone tapasin in peptide optimization of HLA class I molecules Cabrera CMScand J Immunol 2007[Jun]; 65 (6): 487-93During 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.|Animals[MESH]|Antigen Presentation[MESH]|CD8-Positive T-Lymphocytes/metabolism[MESH]|Endoplasmic Reticulum/*metabolism[MESH]|Golgi Apparatus/metabolism[MESH]|Histocompatibility Antigens Class I/genetics/*metabolism[MESH]|Humans[MESH]|Membrane Transport Proteins/genetics/*metabolism[MESH]|Mice[MESH]|Molecular Chaperones/genetics/*metabolism[MESH]|Peptides/*metabolism[MESH]|Protein Binding[MESH]|Protein Disulfide-Isomerases/metabolism[MESH]|Protein Transport[MESH] |
