The final touches make perfect the peptide-MHC class I repertoire.
Major histocompatibility complex (MHC) class I molecules present short, perfectly cleaved peptides on the cell surface for immune surveillance by CD8(+) T cells. The pathway for generating these peptides begins in the cytoplasm, and the peptide-MHC I (pMHC I) repertoire is finalized in the endoplasmic reticulum. Recent studies show that the peptides for MHC I are customized by the ER aminopeptidase associated with antigen processing and by dynamic interactions within the MHC peptide-loading complex. Failure to customize the pMHC I repertoire has profound immunological consequences.
Hammer
Gianna Elena
GE
Division of Immunology, Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720-3200, USA.
Kanaseki
Takayuki
T
Shastri
Nilabh
N
D000818:Animals; D003593:Cytoplasm / Q000276:immunology; D004721:Endoplasmic Reticulum / Q000201:enzymology* / Q000276:immunology; D015395:Histocompatibility Antigens Class I / Q000378:metabolism*; D006801:Humans; D007931:Leucyl Aminopeptidase / Q000172:deficiency / Q000235:genetics / Q000378:metabolism*; D026901:Membrane Transport Proteins / Q000378:metabolism; D010084:Oxidation-Reduction; D010455:Peptides / Q000276:immunology* / Q000378:metabolism*; D019704:Protein Disulfide-Isomerases / Q000378:metabolism*
D015395:Histocompatibility Antigens Class I; D026901:Membrane Transport Proteins; D010455:Peptides; C107762:tapasin; D007931:Leucyl Aminopeptidase; C456799:puromycin-insensitive leucyl-specific aminopeptidase; D019704:Protein Disulfide-Isomerases