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Journal Article

Oxidized phagosomal NOX2 complex is replenished from lysosomes.

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Halder,  P.
Department of Neurobiology, MPI for Biophysical Chemistry, Max Planck Society;

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Supplementary Material (public)

2430287_Suppl.htm
(Supplementary material), 217KB

Citation

Dingjan, I., Linders, P. T. A., van den Bekerom, L., Baranov, M. V., Halder, P., ter Beest, M., et al. (2017). Oxidized phagosomal NOX2 complex is replenished from lysosomes. Journal of Cell Science, 130(7), 1285-1298. doi:10.1242/jcs.196931.


Cite as: http://hdl.handle.net/11858/00-001M-0000-002D-289A-D
Abstract
In dendritic cells, the NADPH oxidase 2 complex (NOX2) is recruited to the phagosomal membrane during antigen uptake. NOX2 produces reactive oxygen species (ROS) in the lumen of the phagosome that kill ingested pathogens, delay antigen breakdown and alter the peptide repertoire for presentation to T cells. How the integral membrane component of NOX2, cytochrome b(558) (which comprises CYBB and CYBA), traffics to phagosomes is incompletely understood. In this study, we show in dendritic cells derived from human blood-isolated monocytes that cytochrome b(558) is initially recruited to the phagosome from the plasma membrane during phagosome formation. Cytochrome b(558) also traffics from a lysosomal pool to phagosomes and this is required to replenish oxidatively damaged NOX2. We identified syntaxin-7, SNAP23 and VAMP8 as the soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) proteins mediating this process. Our data describe a key mechanism of how dendritic cells sustain ROS production after antigen uptake that is required to initiate T cell responses.