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. 2019 May 3;10:534. doi: 10.3389/fphys.2019.00534

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Copyright © 2019 Elu, Osinalde, Beaskoetxea, Ramirez, Lectez, Aloria, Rodriguez, Arizmendi and Mayor.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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USP9X inhibition by WP1130 enhances DDI1 ubiquitination. Cells expressing GFP-DDI1 and FLAG-Ub were treated with 5 μM WP1130 or DMSO for 1 h. GFP-DDI1 was pulled down and its ubiquitination monitored by western blot. Anti-GFP antibody was used to detect unmodified GFP-DDI1 levels whereas anti-FLAG antibody was used to detect ubiquitination. The signal of FLAG was normalized to the GFP signal. Equivalent amount of transfected ubiquitin was detected in the cell lysates by measuring FLAG-Ub levels [Input FLAG-(Ub)]. Quantification using Image-J showed a statistically significant increase in DDI1 ubiquitination after WP1130 treatment [t-test, ^∗p-value < 0.05, (mean ± S.E.M., n = 3)].