title: The double role of the endoplasmic reticulum chaperone tapasin in peptide optimization of HLA class I molecules.
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.
authors.affiliation: Stem Cell Bank of Andalucia (Spanish Central Node), Hospital Universitario Virgen de las Nieves, Granada, Spain. carmenm.cabrera.sspa@juntadeandalucia.es
authors.forename: C M
authors.initials: CM
authors.lastname: Cabrera
mesh_terms: D000818:Animals; D017951:Antigen Presentation; D018414:CD8-Positive T-Lymphocytes / Q000378:metabolism; D004721:Endoplasmic Reticulum / Q000378:metabolism*; D006056:Golgi Apparatus / Q000378:metabolism; D015395:Histocompatibility Antigens Class I / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D026901:Membrane Transport Proteins / Q000235:genetics / Q000378:metabolism*; D051379:Mice; D018832:Molecular Chaperones / Q000235:genetics / Q000378:metabolism*; D010455:Peptides / Q000378:metabolism*; D011485:Protein Binding; D019704:Protein Disulfide-Isomerases / Q000378:metabolism; D021381:Protein Transport
chemical_list: D015395:Histocompatibility Antigens Class I; D026901:Membrane Transport Proteins; D018832:Molecular Chaperones; D010455:Peptides; C107762:tapasin; D019704:Protein Disulfide-Isomerases