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. 2015 Nov 5;26(22):4109–4123. doi: 10.1091/mbc.E14-06-1114

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© 2015 McCabe Pryor, Steinkamp, et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0).

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FIGURE 8: — (A–C) Characterization of the E933Q ErbB3 mutant indicates that changes in off-rate or dephosphorylation do not contribute to gain of function. (A, B) Histograms of dimer lifetimes as revealed by single-particle tracking and HMM analysis of two-color QD-conjugated HA Fab (A) or HRG (B) bound to ^HAErbB3^E933Q receptors on the surface of CHO cells. Unliganded receptor pairs have an off-rate of 0.42/s, which is comparable to the wild-type value. The lifetime of liganded ^HAErbB3^E933Q receptor pairs is also comparable to wild-type receptor at 0.19/s. (C) Normalized ErbB3 PY1289 phosphorylation levels after 2-min stimulation followed by lapatinib treatment (10 μM) in CHO ErbB3^wt vs. CHO ErbB3^E933Q plotted over time. As in Figure 3, phosphorylation levels of both receptors were set to 1 for the 2-min time point after HRG stimulation. Points were fitted to a one-phase exponential decay curve to determine the dephosphorylation half-life. (D) Simulation in BioNetGen for a gain-of-function mutation applied to the activator function, as a function of ligand occupancy. Ratio of 1 ErbB2:20 ErbB3 is used here, since the data reported in Figure 7 were acquired in cells stably expressing ErbB3 in the background of low, endogenous ErbB2.