FYCO1 Recruitment to Dectin-1 Phagosomes is Accelerated by Light Chain 3 Protein and Regulates Phagosome Maturation and Reactive Oxygen Production
| Autor: | Jun Ma, Christopher N. Reyes, David M. Underhill, Courtney A. Becker |
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| Jazyk: | angličtina |
| Rok vydání: | 2014 |
| Předmět: |
Autophagosome
media_common.quotation_subject Phagocytosis Immunology Bone Marrow Cells Biology Article Mice Phagosomes Phagosome maturation Autophagy Immunology and Allergy Animals Guanine Nucleotide Exchange Factors Lectins C-Type RNA Small Interfering Internalization Cells Cultured Phagosome media_common LAMP1 Macrophages Lysosome-Associated Membrane Glycoproteins Dendritic Cells Phosphoproteins Cell biology Mice Inbred C57BL embryonic structures RNA Interference biological phenomena cell phenomena and immunity Reactive Oxygen Species Microtubule-Associated Proteins Intracellular Signal Transduction |
| Popis: | L chain 3 (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’s association with phagosomes has been implicated in regulating microbial killing, Ag processing, and phagosome maturation; however, the mechanism by which LC3 influences these processes has not been clear. In this study, we report that FYVE and coiled–coil domain containing 1 (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+ phagosomes into late LAMP1+ phagosomes. When FYCO1 is lacking, phagosomes stay p40phox+ longer and produce more reactive oxygen. |
| Databáze: | OpenAIRE |
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