Nature Immunology5, 661 - 669 (2004)
Published online: 28 June 2004; | doi:10.1038/ni1090
Generation of major histocompatibility complex class I antigens: functional interplay between proteasomes and TPPII
Peter M Kloetzel
Institut für Biochemie, University Medical School-Charité, Humboldt Universität Monbijoustr.2, 10117 Berlin, Germany. p-m.kloetzel@charite.de
The proteasome is key in the cascade of proteolytic processing required for the generation of peptides presented at the cell surface to cytotoxic T lymphocytes by major histocompatibility complex class I molecules. Proteasome-dependent epitope processing is greatly improved through the interferon--induced formation of immunoproteasomes and the activator complex PA28. Tripeptidyl aminopeptidase II also has a strong effect on epitope generation. With its endoproteolytic and exoproteolytic activities, TPPII acts 'downstream' of the proteasome and relies on products released by the proteasome. The antigen-processing cascade involving different proteolytic systems raises anew the question of how antigenic peptides are generated. We therefore revisit the interferon--induced immune adaptation of the proteasome and attempt to redefine its function in connection with the emerging importance of TPPII.
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-induced formation of immunoproteasomes and the activator complex PA28. Tripeptidyl aminopeptidase II also has a strong effect on epitope generation. With its endoproteolytic and exoproteolytic activities, TPPII acts 'downstream' of the proteasome and relies on products released by the proteasome. The antigen-processing cascade involving different proteolytic systems raises anew the question of how antigenic peptides are generated. We therefore revisit the interferon-
