Fig. 5: phospho-proteomic analysis of Src-ULBR signaling in SW620 cancer cells.
From: Regulation of Src tumor activity by its N-terminal intrinsically disordered region
a A label-free quantitative phospho-proteomic analysis centered on tyrosine phosphorylation. A Veen diagram where quantified phospho-peptides were sorted as differentially phosphorylated from the control condition (mock) (log2FC ≥ 1) in the indicated Src (or Src3A) conditions. b A phospho-RTK array approach. c A phospho-signaling kinase array approach. Comparison of Src (gray boxes) and Src3A (white boxes) induced tyrosine phosphorylation of RTKs and phosphorylation of signaling kinases. Is shown the phosphorylation level of selected kinases relative to the mock condition (fold control; duplicates from 2 independent experiments). d–f Fyn and EPHA2 are important mediators of ULBR-Src signaling in SW620 cancer cells. d, e Biochemical analysis and relative band intensity quantification of p42/44 MAPK and Akt activity in SW620 expressing or not Src or Src3A mutant as shown and transfected with indicated siRNA (n = 3). The level of EPHA2 and Fyn is also shown (n = 2). f Cell invasion of SW620 expressing or not Src or Src3A mutant and transfected with indicated siRNA. The histograms show the percentage of migrating cells in the matrigel matrix normalized to control condition set at 100% (cell invasion). Is shown the mean ± SD; n = 4; ns: p > 0.05; *p < 0.05; **p < 0.01; ***p < 0.001; Student’s t test.
