The final touches make perfect the peptide-MHC class I repertoire

Gianna Elena Hammer; Takayuki Kanaseki; Nilabh Shastri

doi:10.1016/j.immuni.2007.04.003

The final touches make perfect the peptide-MHC class I repertoire

Immunity. 2007 Apr;26(4):397-406. doi: 10.1016/j.immuni.2007.04.003.

Authors

Gianna Elena Hammer¹, Takayuki Kanaseki, Nilabh Shastri

Affiliation

¹ Division of Immunology, Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720-3200, USA.

PMID: 17459809
DOI: 10.1016/j.immuni.2007.04.003

Abstract

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.

Publication types

Research Support, N.I.H., Extramural
Review

MeSH terms

Animals
Cytoplasm / immunology
Endoplasmic Reticulum / enzymology*
Endoplasmic Reticulum / immunology
Histocompatibility Antigens Class I / metabolism*
Humans
Leucyl Aminopeptidase / deficiency
Leucyl Aminopeptidase / genetics
Leucyl Aminopeptidase / metabolism*
Membrane Transport Proteins / metabolism
Oxidation-Reduction
Peptides / immunology*
Peptides / metabolism*
Protein Disulfide-Isomerases / metabolism*

Substances

Histocompatibility Antigens Class I
Membrane Transport Proteins
Peptides
tapasin
Leucyl Aminopeptidase
puromycin-insensitive leucyl-specific aminopeptidase
Protein Disulfide-Isomerases