SWAP70 Organizes the Actin Cytoskeleton and Is Essential for Phagocytosis
Cell Reports, ISSN: 2211-1247, Vol: 17, Issue: 6, Page: 1518-1531
2016
- 45Citations
- 89Captures
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
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Metrics Details
- Citations45
- Citation Indexes45
- 45
- CrossRef34
- Captures89
- Readers89
- 89
Article Description
Actin plays a critical role during the early stages of pathogenic microbe internalization by immune cells. In this study, we identified a key mechanism of actin filament tethering and stabilization to the surface of phagosomes in human dendritic cells. We found that the actin-binding protein SWAP70 is specifically recruited to nascent phagosomes by binding to the lipid phosphatidylinositol (3,4)-bisphosphate. Multi-color super-resolution stimulated emission depletion (STED) microscopy revealed that the actin cage surrounding early phagosomes is formed by multiple concentric rings containing SWAP70. SWAP70 colocalized with and stimulated activation of RAC1, a known activator of actin polymerization, on phagosomes. Genetic ablation of SWAP70 impaired actin polymerization around phagosomes and resulted in a phagocytic defect. These data show a key role for SWAP70 as a scaffold for tethering the peripheral actin cage to phagosomes.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S2211124716314073; http://dx.doi.org/10.1016/j.celrep.2016.10.021; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=84995579393&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/27806292; https://linkinghub.elsevier.com/retrieve/pii/S2211124716314073
Elsevier BV
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