Reference - Detail
| RRC ID | 52564 |
|---|---|
| Author | Egami Y, Araki N. |
| Title | Transient recruitment of M-Ras GTPase to phagocytic cups in RAW264 macrophages during FcγR-mediated phagocytosis. |
| Journal | Microscopy (Oxf) |
| Abstract |
M-Ras, a member of the Ras superfamily, is known to be involved in diverse cellular processes. However, its involvement in FcγR-mediated phagocytosis remains unknown. We examined the spatiotemporal localization of M-Ras during the engulfment of IgG-opsonized erythrocytes (IgG-Es) in RAW264 macrophages. By the live-cell imaging of fluorescent protein-fused M-Ras, we found that M-Ras was localized to the membrane of phagocytic cups during the early stage of phagosome formation. Notably, ratiometric image analysis revealed that M-Ras was concentrated in the membrane of forming phagosomes. Moreover, our analysis of M-Ras mutant expression showed that phagosome formation was significantly inhibited in cells expressing GDP-locked mutant M-Ras-S27N. In contrast, the expression of wild-type M-Ras or GTP-locked mutant M-Ras-G22V facilitated the uptake of IgG-Es. These data suggest that M-Ras is a novel component of the FcγR-mediated phagocytic pathway and may regulate phagosome formation in macrophages. |
| Volume | 67(2) |
| Pages | 68-74 |
| Published | 2018-4-1 |
| DOI | 10.1093/jmicro/dfx131 |
| PII | 4797532 |
| PMID | 29340604 |
| MeSH | Animals Cell Line Cell Membrane / immunology Erythrocytes / immunology* Immunoglobulin G / immunology Macrophages / immunology* Mice Monomeric GTP-Binding Proteins / metabolism* Phagocytosis / immunology* Phagosomes / immunology Protein Binding / immunology RAW 264.7 Cells Receptors, IgG / immunology* ras Proteins |
| IF | 1.394 |
| Times Cited | 1 |
| Altmetric score |
オルトメトリクス指標項目
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| The most frequently cited source | |
| Total number of mentions | 1 |
| Altmetric score changes over past 6months | 0.0 |
| Resource | |
| Human and Animal Cells | RAW 264(RCB0535) |