A. Cartoon schematic depicting nanobody inhibition of activation by lipidated Gβγ (1.5 μM final concentration). Lipid kinase assays show a potent inhibition of lipid kinase activity with increasing concentrations of NB7 (3–3000 nM) for the different complexes. The protein concentration of p110γ (300 nM), p110γ-p84 (330 nM) and p110γ-p101 (12 nM) was different due to intrinsic differences of each complex to be activated by lipidated Gβγ.
B. Association and dissociation curves for the dose response of His-NB7 binding to p110γ, p110γ-p84 and p110γ-p101 (50 – 1.9 nM) is shown. A cartoon schematic of BLI analysis of the binding of immobilized His-NB7 to p110γ is shown on the left. Dissociation constants (KD) were calculated based on a global fit to a 1:1 model for the top three concentrations and averaged with error shown.
B. Association and dissociation curves for His-NB7 binding to p110γ, p110α-p85 α, p110β-p85β, and p110δ-p85β. Experiments were performed in duplicate with a final concentration of 50 nM of each class I PI3K complex.
D. Total Internal Reflection Fluorescence Microscopy (TIRF-M) analysis of the effect of nanobody NB7 on PI3K recruitment to supported lipid bilayers containing H-Ras(GTP) and farnesyl-Gβγ. Y647-p84/p110γ displays rapid equilibration kinetics and is insensitive to the addition of 500 nM nanobody (black arrow, 250 sec) on supported lipid bilayers containing H-Ras(GTP) and farnesyl-Gβγ.
E. Kinetics of 50 nM DY647-p84/p110γ membrane recruitment appears indistinguishable in the absence and presence of nanobody. Prior to sample injection, DY647-p84/p110γ was incubated for 10 minutes with 500 nM nanobody.
F. Representative TIRF-M images showing the localization of 50 nM DY647-p84/p110γ visualized in the absence or presence of 500 nM nanobody (+NB7). Membrane composition for panels C-E: 93% DOPC, 5% DOPS, 2% MCC-PE, Ras(GTP) covalently attached to MCC-PE, and 200 nM farnesyl-Gβγ.