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. 2017 Apr 15;28(8):1066–1078. doi: 10.1091/mbc.E16-05-0285

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© 2017 Lovelace 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 5: — Depletion of ARHGAP18 from ECs results in decreased MT stability. (A) ECs were transfected with control siRNA (siC; ■) or siRNA for ARGAP18 (siGAP18; □) and analyzed after 48 h for Ac-Tub or glu-tubulin expression. Western blot is representative of a single HUVEC line. Densitometry analysis of protein expression normalized to untreated control. Results are ± SEM; three independent HUVEC lines in duplicate; *p < 0.05. (B) Analysis of ARHGAP18 in ARHGAP18-overexpressing cells. Overexpression was achieved by infecting HUVECs with ARHGAP18-containing adenovirus. After 48 h, the lysates were analyzed for Ac-Tub expression. Western blot is representative of a single HUVEC line. Densitometry analysis of protein expression normalized to untreated control. Results are ± SEM; three independent HUVEC lines in duplicate; *p < 0.05. (C) ECs were transfected with control siRNA (siC) or siRNA for ARGAP18 (siGAP18), lysed after 48 h, and soluble and polymerized tubulin fractions were separated as given in Materials and Methods. Fractions were then analyzed by Western blotting and probed for ARHGAP18 and α-tubulin. (i) Representative Western blot and comparative densitometry levels of ARHGAP18 in soluble and polymerized fractions from control or ARHGAP18-depleted cells. Densitometry readings from three independent experiments. The levels of ARHGAP18 in the siC cells in both the soluble and polymerized fractions are normalized to 1.0. Representative of three independent experiments. P, polymerized tubulin fraction; S, soluble tubulin fraction. (ii) Percentage of polymerized tubulin. Mean ± SEM, *p < 0.05.