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. 2018 Jan 2;217(1):329–346. doi: 10.1083/jcb.201702179

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© 2018 Naufer et al.

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Figure 9. — The Vps34 complex II association to phagosomes is controlled by pH. (a) Vps34 complex II subunits in isolated latex beads phagosomes. RAW macrophages in culture media (control), acidic culture media (pH 4.0), or cell-culture medium with 10 mM NH₄Cl were allowed to internalize IgG-opsonized latex beads for 20 min. After this period, phagosomes were isolated and immunoblotted for the presence of Vps15, UVRAG, Vps34, Raptor, and Rab7. Human IgG was used as a control for number of phagosomes loaded. (b) Protein densitometric quantification for blots shown in panel a. Human IgG was used to normalize phagosomal loading. Data shown are means ± SEMs from four to six independent experiments; *, P < 0.05; **, P < 0.01. (c) Phos-Tag SDS-PAGE determination of the phosphorylation states of UVRAG, Vps34, and Vps15 in phagosomes isolated as described in panel a. (d) The phosphorylation coefficient was used to quantify the preferred states of phosphorylation. This was done by calculating an internal ratio of the most (top) to least (bottom) phosphorylated species. Data shown are means ± SEMs from three or four independent experiments. *, P < 0.05.