Abstract
The recruitment of endoplasmic reticulum (ER) components to dendritic cell (DC) phagosomes and endosomes is a crucial event to achieve efficient cross-presentation of exogenous antigens. We have previously identified the small GTPase Rab22a as a key regulator of MHC-I trafficking and antigen cross-presentation by DCs. In this study we show that low expression of Rab22a does not prevent the normal delivery of ER-derived proteins to DC phagosomes. In contrast, the presence of these proteins was diminished in endosomes labelled with a fluid phase marker. These observations were confirmed by a functional assay that assesses the translocation of a soluble protein to the cytosol. Interestingly, we also demonstrate that early endosomal maturation is altered in Rab22a deficient DCs. Our results indicate that Rab22a plays a major role in endosomal function and highlight the importance of studying the endocytic and phagocytic pathways separately in DCs.