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. Author manuscript; available in PMC: 2017 Apr 19.
Published in final edited form as: Biochemistry. 2016 Apr 11;55(15):2269–2277. doi: 10.1021/acs.biochem.5b01287

Figure 4. Cancer-Associated SHP2 Mutations Increase Basal Phosphatase Activity and Sensitivity to IRS-1 Phosphopeptide ligand Stimulation.

Figure 4

(A) Schematic illustrating DiFMUP dephosphorylation by SHP2. (B) Basal enzymatic trajectories of wild-type and cancer-associated SHP2 proteins across varying concentrations of DiFMUP. (C) Enzymatic activity of SHP2 proteins (0.05 nM) across varying concentrations of an IRS-1-derived monophosphorylated peptide. (D) Identical experiment to C but with synthetic bisphosphorylated peptide derived from IRS-1. (E) Phosphatase activity of SHP2 proteins (0.01 nM) at saturating concentrations of a double-phosphorylated peptide derived from IRS-1 (6 μM) across varying concentrations of DiFMUP. Velocity data is shown as mean ± standard deviation and was fit to the standard Michaelis-Menten equation to extrapolate kcat and KM values.