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. 2021 Apr 21;40(10):e106188. doi: 10.15252/embj.2020106188

Figure 3. Tpl2[D270A] mutation alters the protein composition of phagosomes.

Figure 3

WT and Tpl2[D270A] BMDMs were incubated with latex beads for 0.5 h. Latex bead phagosomes were purified from Tpl2[D270A] and WT BMDMs and analysed by mass spectrometry. Biological triplicates were analysed for each genotype.
  1. Heatmap of selected proteins that were significantly downregulated in BMDMs from Tpl2[D270A] mice relative to WT (P < 0.05). Selected hits were grouped into clusters according to their molecular functions.
  2. Gene set enrichment analysis (GSEA) of significantly downregulated biological processes in phagosomal fractions. Changes of Tpl2[D270A] phagosomes relative to WT. Dot colour; enrichment score. Dot size; statistical significance.
  3. Protein intensities of V‐ATPase subunits from phagosomes purified from WT and Tpl2[D270A] BMDMs, (n = 3 biological replicates).
  4. Protein intensities of RAB5 and LAMP‐1 from phagosome proteome analysis of WT and Tpl2[D270A] BMDMs (n = 3 biological replicates) (left). Immunoblot of isolated phagosomes from WT and Tpl2[D270A] BMDMs probed for RAB5, LAMP‐1, and vimentin. Phagosomal fractions of two biological replicates were pooled. One representative experiment out of two shown (right) (n = 2).

Data information: Data were analysed by Student’s t‐test. Error bars represent SEM. *P < 0.05, **P < 0.01, ***P < 0.001, ****P < 0.0001.