Sec22b in cross-presentation

Abstract

volume 13 number 2 february 2012 nature immunology Sec22b in cross-presentation The cross-presentation of exogenous peptides is necessary for priming efficient antiviral and antitumor immune responses. Specific dendritic cell subsets specialize in cross-presentation, but how this process allows antigen processing and loading of antigen onto major histocompatibility complex class I molecules remains unclear. In Cell, Cebrian et al. show that phagosomes in dendritic cells fuse with endoplasmic reticulum– Golgi transport vesicles via a fusogenic SNARE complex composed of Sec22b and syntaxin 4. Sec22b is located on the membranes of transport vesicles that move cargo between the endoplasmic reticulum and cisGolgi compartments and can capture syntaxin 4 present on phagosomes, which allows mixing of membrane proteins, including peptide-loading machinery dependent on the transporter TAP. Cells that lack Sec22b fail to cross-present antigen to CD8+ T cells, which demonstrates the requirement for endoplasmic reticulum–phagosome vesicle fusion in this antigen-presentation process. How this Sec22b-dependent intracellular trafficking is regulated is unknown. LAD Cell 147, 1355–1368 (2011) Inhibiting ubiquitin sensing

DOI: 10.1038/ni.2221

Cite this paper

@article{Dempsey2012Sec22bIC, title={Sec22b in cross-presentation}, author={Laurie A. Dempsey}, journal={Nature Immunology}, year={2012}, volume={13}, pages={120-120} }