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The Double Role of the Endoplasmic Reticulum Chaperone Tapasin in Peptide Optimization of HLA Class I Molecules
Author(s) -
Cabrera C. M.
Publication year - 2007
Publication title -
scandinavian journal of immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.934
H-Index - 88
eISSN - 1365-3083
pISSN - 0300-9475
DOI - 10.1111/j.1365-3083.2007.01934.x
Subject(s) - transporter associated with antigen processing , endoplasmic reticulum , antigen presentation , human leukocyte antigen , microbiology and biotechnology , antigen processing , chaperone (clinical) , peptide , stim1 , cd8 , mhc class i , chemistry , biology , antigen , biochemistry , t cell , immunology , immune system , medicine , pathology
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.