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. 2016 Feb 1;27(3):434–441. doi: 10.1091/mbc.E15-07-0546

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© 2016 Fisher 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: — Et/Lat is trafficked and degraded in the lysosome via a slower mechanism than that for Dome. (A) Time course of receptor degradation over the indicated time in hours. Cyclohexamide to block new translation and Upd2-conditioned medium were present throughout the assay. (A′) Quantification of data shown in A after normalization of FLAG to α-tubulin (Dome-FLAG, dashed line; Et/Lat-FLAG, solid line). (B) Levels of Dome-FLAG and Et/Lat-FLAG 10 h after the addition of cyclohexamide and Upd2 ligand stimulation. By comparison to the dimethyl sulfoxide carrier control, incubation with 0.2 μM bafilomycin A1 greatly reduced ligand-induced degradation of Dome and Et/Lat, whereas treatment with 10 μM MG132 did not. (B′) Quantification of data shown in B. (C) Time course of Dome-FLAG and Et/Lat-FLAG degradation over the indicated time course after prior treatment with dsRNA targeting the indicated mRNAs. (C′) Quantification of receptor levels normalized to α-tubulin and shown by solid lines (Et/Lat-FLAG) and dashed lines (Dome-FLAG). (D) Steady-state levels of Dome:Dome (DD), Dome:Et/Lat (DL), and Et/Lat:Et/Lat (LL) dimers as reported by the βlue-βlau bimolecular complementation and β-Glo assay after 5 d of RNAi treatment. Results are shown as fold changes to control. Control levels were averaged from two wells treated with rh5 dsRNA. Significant results are shown; all unlabeled bars were not significantly different from controls. *p < 0.05, **p < 0.01, ***p < 0.001.