Figure 1: Type II IL-4 receptor dynamics and dimerization quantified in vitro. | Nature Communications

Figure 1: Type II IL-4 receptor dynamics and dimerization quantified in vitro.

From: Ligand-induced type II interleukin-4 receptor dimers are sustained by rapid re-association within plasma membrane microcompartments

Figure 1

(a) Two-step dimerization of the type II IL-4 receptor by different ligands. Top: binding of IL-4 to IL-4Rα followed by recruitment of IL-13Rα1 at the membrane. For IL-4 mutants with altered affinities to IL-13Rα1, changes in the equilibrium between binary and ternary complexes are expected. Bottom: binding of IL-13 to IL-13Rα1 followed by recruitment of IL-4Rα. (b) Typical binding assay showing association (highlighted in grey) and dissociation of AT488IL-4D interaction with IL-4Rα-EC and IL-13Rα1-EC tethered on an SSM (TIRFS signal only, full TIRFS-RIf experiment shown in Supplementary Fig. 6). The dissociation curve was fitted (black curve) by using a two-step disassembly model (inset cartoon) to obtain the two-dimensional association rate constant . (c) Comparison of the dissociation kinetics observed for AT488IL-4D interacting with IL-4Rα-EC (1.3 fmol mm−2) in absence of IL-13Rα1-EC and in presence of different IL-13Rα1-EC surface concentrations (ratios are indicated at the curves). (d) Comparison of the dissociation kinetics obtained for AT488KFRD (green), OG488IL-13 (light red), AT488IL-4D (violet), AT488RGAD (orange) and AT488DND (blue). Binary complex dissociation kinetics of AT488IL-4D↔IL-4Rα-EC (dark rose) and OG488IL-13↔IL-13Rα1-EC (red) are also depicted.

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