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. 2023 Oct 17;24(20):15257. doi: 10.3390/ijms242015257

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© 2023 by the authors.

Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).

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USP17 increases Osx protein stability by suppressing Osx ubiquitination. (a,b) HEK 293 cells were transfected with HA-Osx, Myc-USP17, and Myc-USP17-CS. After transfection, the cells were treated with CHX (40 μg/mL) for the indicated time. The protein levels of Osx, Myc-USP17, and tubulin were detected by IB. The intensities of protein (Osx) were quantified by Image J Version 1.52k. ns, not significant. *** p < 0.001 compared to the control group. (c) HEK 293 cells were transfected with HA-Osx, Flag-Ub, Myc-USP17, and Myc-USP17-CS. The ubiquitination of Osx was detected by IP and measured by IB.