Fig. 6 | Scientific Reports

Fig. 6

From: HMMR has oncoprotein-like properties in neuroblastoma cells and high HMMR expression has independent prognostic potential in neuroblastomas

Fig. 6

Functional activity of the HMMR phosphoproteomic signature. (A) Phosphopeptide differences between cell lines and KELLY, observed in components of the MTOR regulatory network. Red and blue show log2-fold increased or decreased phosphorylation, respectively; white is no change (* P < 0.05, ** P < 0.01, *** P < 0.001). (B) KSEA analysis of differentially phosphorylated peptides in the whole dataset, showing those most relevant to MTOR signaling. (C) Immunoblot analysis of cell lines for phosphorylated ERK (P-T185/P-Y187 (ERK2) or P-T202/P-Y204 (ERK1)), AKT (S473), and Aurora A as well as HMMR and CD44 (n = 3); original data in Supplementary Fig. S8. (D) Protein signals were normalised to either their respective total proteins or GAPDH, and then expressed as a mean ± SD; *P ≤ 0.05, **p < 0.005. (E) Examples of MAPK3 (ERK1) and MAPK1 (ERK2) substrates are shown as protein networks based on STRING and visualised in Cytoscape. Inner and outer rings represent kinase activity status (z score). Red and blue colour indicate increased or decreased kinase activity, respectively, with greater colour intensity reflecting greater z scores.

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