Functional significance of tapasin membrane association and disulfide linkage to ERp57 in MHC class I presentation.
Tapasin is disulfide linked to ERp57 within the peptide loading complex. In cell-free assays, a soluble variant of the tapasin/ERp57 dimer recruits MHC class I molecules and promotes peptide binding to them, whereas soluble tapasin alone does not. Here we show that within cells, tapasin conjugation with ERp57 is as critical as its integration into the membrane for efficient MHC class I assembly, surface expression, and Ag presentation to CD8(+) T cells. Elimination of both of these properties severely compromises tapasin function, in keeping with predictions from in vitro studies.
Vigneron
Nathalie
N
Department of Immunobiology, Howard Hughes Medical Institute, Yale University School of Medicine, New Haven, CT 06520-8011, USA.
Peaper
David R
DR
Leonhardt
Ralf M
RM
Cresswell
Peter
P
D017951:Antigen Presentation / Q000276:immunology*; D002460:Cell Line; D002462:Cell Membrane / Q000276:immunology* / Q000378:metabolism; D015395:Histocompatibility Antigens Class I / Q000276:immunology / Q000378:metabolism*; D006801:Humans; D026901:Membrane Transport Proteins / Q000276:immunology / Q000378:metabolism*; D011485:Protein Binding / Q000276:immunology; D019704:Protein Disulfide-Isomerases / Q000276:immunology / Q000378:metabolism*; D013602:T-Lymphocytes, Cytotoxic / Q000276:immunology* / Q000378:metabolism
D015395:Histocompatibility Antigens Class I; D026901:Membrane Transport Proteins; C107762:tapasin; D019704:Protein Disulfide-Isomerases; C085868:PDIA3 protein, human
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