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. 2017 Sep 13;7:11480. doi: 10.1038/s41598-017-11915-5

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© The Author(s) 2017

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Schematic representation of the role of 3BP2 on FcγR-mediated signalling and the physiological relevance of Syk-dependent phosphorylation. IgG-coated pathogenic particles induce cross-linking of Fc gamma RI (FcγRI), which forms a protein complex with Fc receptor γ (FcRγ) to activate Syk. The activation of Syk triggers various signalling cascades to promote phagocytosis and gene expression. Syk-dependent tyrosine phosphorylation of 3BP2 (P) is critical for optimal FcRγ-mediated phagocytosis and chemokine mRNA expression.