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. 2019 Jan 27;15(7):1130–1149. doi: 10.1080/15548627.2019.1570063

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© 2019 The Author(s). Published by Informa UK Limited, trading as Taylor & Francis Group.

This is an Open Access article distributed under the terms of the Creative Commons Attribution-NonCommercial-NoDerivatives License (http://creativecommons.org/licenses/by-nc-nd/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited, and is not altered, transformed, or built upon in any way.

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Figure 3. — SMURF1-mediated UVRAG ubiquitination does not affect its stability. (a) No apparent change of UVRAG protein levels was detected in SMURF1-overexpressing or SMURF1-depleted cells. HEK293T cells were transfected with indicated siRNAs (lower) or plasmids (upper), and endogenous proteins were examined by western blotting. (b) MG132 did not change SMURF1-mediated UVRAG ubiquitination levels. In vivo ubiquitination assays were performed in HEK293T cells transfected with the indicated plasmids. Cells were treated with DMSO or MG132 (15 μM) for 4 h before harvest. (c) SMURF1 did not affect the turnover of UVRAG protein. HEK293T cells transfected with the indicated plasmids were treated with 15 μg/ml cycloheximide (CHX) for various times, and endogenous UVRAG was analyzed by western blotting. The graph in panel C represents the results from three independent experiments. (d) SMURF1 did not affect the levels of UVRAG mRNA. HEK293T cells were transfected with the indicated plasmids, and endogenous UVRAG was analyzed by qRT-PCR and shown.