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[Preprint]. 2023 May 23:2023.04.12.536585. Originally published 2023 Apr 12. [Version 2] doi: 10.1101/2023.04.12.536585

Figure 4. Activating phosphorylation at the helical domain leads to opening of the regulatory motif.

Figure 4.

A. HDX-MS comparing apo and phosphorylated p110γ. Significant differences in deuterium exchange are mapped on to the structure and cartoon of p110γ according to the legend (PDB: 7MEZ).

B. The graph of the #D difference in deuterium incorporation for p110γ, with each point representing a single peptide. Peptides colored in red are those that had a significant change in the mutants (greater than 0.4 Da and 5% difference at any timepoint, with a two tailed t-test p<0.01). Error bars are S.D. (n=3).

C. Representative bimodal distribution (EX1 kinetics) observed in the helical domain peptides of p110γ.

D. Representative p110γ peptides displaying increases in exchange in the phosphorylated state are shown. For all panels, error bars show SD (n = 3)

E. Measurement of ATP to ADP conversion of phosphorylated and non-phosphorylated p110γ (1000 nM final concentration) ATPase activity in the absence (left) and presence of PIP2 membranes (5% phosphatidylinositol 4,5-bisphosphate (PIP2), 95% phosphatidylserine (PS)) activation (right). Significance is indicated by **(<0.001%), and ***(<0.0001%).