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. 2017 Jan 1;28(1):128–140. doi: 10.1091/mbc.E16-06-0451

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© 2017 Levin et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0).

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FIGURE 2: — Comparison of the changes in PtdIns4P content to those of PtdIns(4,5)P₂ and PtdIns3P. (A) Time-lapse gallery of confocal micrographs of RAW264.7 cells coexpressing GFP-2xP4M and mRFP-PH-PLCδ, a PtdIns(4,5)P₂ biosensor, during phagocytosis of IgG-SRBCs. (B) Time-lapse gallery of confocal micrographs of cells coexpressing GFP-2xP4M and mRFP-2xFYVE-EEA1, a PtdIns3P biosensor, during phagocytosis of IgG-SRBCs. Insets, magnifications of the area delimited by dotted white boxes; dashed circles show the location of the phagosome. Scale bars, 5 μm. (C) Time course of the changes in PtdIns4P and PtdIns(4,5)P₂ during phagosome formation. The intensity of GFP-2xP4M fluorescence in the phagosome was measured and normalized to the plasmalemmal intensity; to enable comparison between cells and between experiments, the data are expressed relative to the maximum value (green line, white circles). A similar analysis was applied to mRFP-PH-PLCδ (red line, black circles), a PtdIns(4,5)P₂ biosensor. (D) Time course of the changes in PtdIns4P and PtdIns3P during phagosome formation and maturation. PtdIns4P was monitored as before, using GFP-2xP4M. mCh-FYVE-EEA1 was used as a PtdIns3P probe; phagosomal intensity was measured after subtracting cytosolic fluorescence. Data are expressed relative to the maximum value. Values are means ± SEM of three and five independent experiments, respectively. Note the different time scales used in C vs. D. Initial contact between cells and IgG-SRBC was considered as time 0.