Cutting edge: FYCO1 recruitment to dectin-1 phagosomes is accelerated by light chain 3 protein and regulates phagosome maturation and reactive oxygen production.

Cutting edge: FYCO1 recruitment to dectin-1 phagosomes is accelerated by light chain 3 protein and regulates phagosome maturation and reactive oxygen production.
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DOI:
10.4049/jimmunol.1302835
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发表时间:
2014-02-15
期刊:
Journal of immunology (Baltimore, Md. : 1950)
影响因子:
--
通讯作者:
Underhill DM
Underhill DM
中科院分区:
其他
文献类型:
--
作者:
Ma J;Becker C;Reyes C;Underhill DM

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LC3-associated phagocytosis is a process in which LC3, a protein canonically involved in engulfing intracellular materials (autophagy), is recruited to traditional phagosomes during internalization of extracellular payloads. LC3 association with phagosomes has been implicated in regulating microbial killing, antigen processing, and phagosome maturation, however the mechanism by which LC3 influences these processes has not been clear. In this study, we report that FYCO1, a protein previously implicated in autophagosome trafficking, is recruited directly by LC3 to Dectin-1 phagosomes. During LC3-associated phagocytosis, FYCO1 recruitment facilitates maturation of early p40phox-positive phagosomes into late LAMP1-positive phagosomes. When FYCO1 is lacking, phagosomes stay p40phox-positive longer and produce more reactive oxygen.
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