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  Oxidized phagosomal NOX2 complex is replenished from lysosomes.

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.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002D-289A-D Version Permalink: http://hdl.handle.net/21.11116/0000-0001-57E4-C
Genre: Journal Article

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 Creators:
Dingjan, I., Author
Linders, P. T. A., Author
van den Bekerom, L., Author
Baranov, M. V., Author
Halder, P.1, Author              
ter Beest, M., Author
van den Bogaart, G., Author
Affiliations:
1Department of Neurobiology, MPI for Biophysical Chemistry, Max Planck Society, ou_578595              

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Free keywords: NOX2, SNARE, Phagocytosis dendritic cell, Reactive oxygen species, Phagosome maturation
 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.

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Language(s): eng - English
 Dates: 2017-04-012017-04
 Publication Status: Published in print
 Pages: -
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 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.1242/jcs.196931
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Title: Journal of Cell Science
Source Genre: Journal
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Pages: - Volume / Issue: 130 (7) Sequence Number: - Start / End Page: 1285 - 1298 Identifier: -