Abstract
Peptide epitopes presented by MHC class I molecules are produced through sequential proteolysis, frequently terminating with an aminoterminal trimming step. While the trimming enzymes processing endogenous MHC class I ligands in the endoplasmic reticulum have by now been characterized extensively, we have only recently identified an endosomal enzyme, insulin-regulated aminopeptidase (IRAP) that can trim cross-presented peptides derived from proteins internalized by dendritic cells. Here we summarize the essential features of IRAP as a trimming enzyme, propose an updated model of cellular cross-presentation pathways, and discuss potential additional functions of IRAP and its compartment in dendritic cell biology.
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