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Fig. 1 | Molecular Cancer

Fig. 1

From: Phosphoproteomic analysis reveals Smarcb1 dependent EGFR signaling in Malignant Rhabdoid tumor cells

Fig. 1

Phosphoproteomic profiling reveals robust Smarcb1 dependent changes in protein phosphorylation. Matching Smarcb1 proficient and deficient tumor cells were generated by re-introducing SMARCB1 (pMIG- Smarcb1) or an empty vector as control (pMIG) [14]. a The outline of the phosphoproteomic study. Two triple-SILAC experiments were conducted. The first set allowed evaluation of Smarcb1 dependent changes when cultured in normal serum whilst the second set allowed for the evaluation under serum starvation. Smarcb1 proficient cells grown in normal serum and light isotopic labeling were included in both sets to allow comparison between the two sets. b Western blot demonstrating differential AKT phosphorylation in Smarcb1 deficient versus proficient cells. Bar graph shows quantification of western blot presented as fold change in AKT phosphorylation in pMIG/Smarcb1 cells normalized to beta-actin. c Volcano plot depicting Smarcb1 dependent changes in site phosphorylation across the two sets. X-axis is the log2 ratio of the abundances of specific residues between Smarcb1 proficient and deficient cells. Negative values for highly phosphorylated in Smarcb1 deficient cells. Y-axis is the logarithmic scale for the P-value of the fold change. For P.Vā€‰<ā€‰0.05; Violet dataset represents residues altered in high serum; Green dataset represents residues altered under serum starvation. d Venn-diagram portraying the residues found to be differentially phosphorylated in a Smarcb1-dependent manner. Under 10Ā % serum, 458 residues are highly phosphorylated in Smarcb1 proficient cells (In red) whilst 434 residues are highly phosphorylated in Smarcb1 deficient cells (In blue). Under low serum, 384 residues (roughly two thirds) are highly phosphorylated in Smarcb1 proficient cells, whilst 233 residues are highly phosphorylated in Smarcb1 deficient cells. Overall 205 residues are differentially phosphorylated between Smarcb1 proficient and deficient cells regardless of the serum conditions

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