The Group II chaperonin TRiC protects proteolytic intermediates from degradation in the MHC class I antigen processing pathway

Jun Kunisawa, Nilabh Shastri

Research output: Contribution to journalArticlepeer-review

Abstract

MHC class I molecules present precisely cleaved peptides of intracellular proteins on the cell surface. For most antigenic precursors, presentation requires transport of peptide fragments into the ER, but the nature of the cytoplasmic peptides and their chaperones is obscure. By tracking proteolytic intermediates in living cells, we show that intracellular proteolysis yields a mixture of antigenic peptides containing only N-terminal flanking residues for ER transport. Some of these peptides were bound to the group II chaperonin TRiC and were protected from degradation. Destabilization of TRiC by RNA interference inhibited the expression of peptide-loaded MHC I molecules on the cell surface. Thus, the TRiC chaperonin serves a function in protecting proteolytic intermediates in the MHC I antigen processing pathway.

Original languageEnglish (US)
Pages (from-to)565-576
Number of pages12
JournalMolecular cell
Volume12
Issue number3
DOIs
StatePublished - Sep 1 2003

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

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