Cookies on this website
We use cookies to ensure that we give you the best experience on our website. If you click 'Continue' we'll assume that you are happy to receive all cookies and you won't see this message again. Click 'Find out more' for information on how to change your cookie settings.

Protein degradation by the proteasome releases peptides that can be loaded on MHC class I molecules and presented to cytolytic T lymphocytes. Several mechanisms were recently found to increase the diversity of antigenic peptides displayed at the cell surface, thereby maximizing the efficacy of immune responses. The proteasome was shown to produce spliced antigenic peptides, which are made of two fragments initially not contiguous in the parental protein. Different proteasome subtypes also produce distinct sets of antigenic peptides: the standard proteasome and the immunoproteasome, containing different catalytic subunits, have different cleavage specificities and produce different sets of peptides. Moreover, recent work confirmed the existence of two additional proteasome subtypes that are intermediate between the standard and the immunoproteasome, and each produce a unique peptide repertoire.

Original publication

DOI

10.1016/j.coi.2011.12.002

Type

Journal article

Journal

Curr Opin Immunol

Publication Date

02/2012

Volume

24

Pages

84 - 91

Keywords

Animals, Antigen Presentation, Antigenic Variation, Antigens, Neoplasm, Histocompatibility Antigens Class I, Humans, Isoenzymes, Neoplasm Proteins, Proteasome Endopeptidase Complex, Protein Processing, Post-Translational