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. 2015 Dec 1;26(24):4412–4426. doi: 10.1091/mbc.E15-02-0087

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© 2015 Li 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 4: — The interaction between GGA3 and TrkA is independent of TrkA activation and ubiquitination. (A) Interaction of TrkA and GGA3 in PC12 (615) cells incubated with or without 10 ng/ml NGF for 10 min. Lysates were immunoprecipitated with GGA3 antibody and immunoblotted as shown. (B) Immunoprecipitation of TrkA from HEK293T cells transfected with a TrkA wild type, TrkA kinase-dead mutant (TrkA-K547A), GGA3 wild type, or GGA3 mutant unable to bind ubiquitin (GGA3-L276A) and immunoblotted as shown. (C) Analysis of TrkA recycling in GGA3-depleted PC12 (615) cells rescued with control cDNA (vector) or siRNA-resistant GGA3 wild type or mutant GGA3-L276A. Recycling assays were performed as described in Figure 3A. int, internalized biotinylated TrkA before rewarming; rec, remaining biotinylated receptors after 45 min of rewarming (recycling). (D) Quantification of the degree of TrkA recycling from three independent experiments (as described in C). The amount of recycled TrkA is expressed as the percentage of the pool of biotinylated TrkA after the 7-min internalization period and before rewarming. One-way ANOVA, *p < 0.05, **p < 0.01.