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[Preprint]. 2024 Apr 9:2023.07.10.548257. Originally published 2023 Jul 10. [Version 4] doi: 10.1101/2023.07.10.548257

Figure 6. T42A-dependent changes in the activation of full-length SHP2.

Figure 6.

(A) Measurement of SHP2 activation by phosphopeptides. (B) Representative activation curves for SHP2WT (N = 3–17). (C) Correlation between the EC50 of SHP2WT activation by phosphopeptides and the KD of those phosphopeptides for the N-SH2WT domain (N = 3–4 for KD values, N = 3–17 for EC50 values). (D) Activation EC50 values for SHP2WT versus SHP2R138Q (N = 3–17 for SHP2WT, N = 3–5 for SHP2R138Q). (E) Comparison of SHP2WT and SHP2T42A activation by PD-1 pTyr 248 (N = 3–4). (F) Comparison of SHP2WT and SHP2T42A activation by Imhof-9 (N = 6–17). (G) Bubble plot juxtaposing the EC50 values for activation of SHP2WT and SHP2T42A by nine peptides, alongside the fold-change in KD for binding of those peptides to N-SH2WT vs N-SH2T42A. The dotted line indicates where EC50 for SHP2WT equals EC50 for SHP2T42A. Peptides with a large fold-change in binding affinity (larger bubble) have a large fold-change in EC50 values for SHP2T42A over SHP2WT (distance from dotted line). All EC50 values and p-values can be found in Table S5.