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. 2020 Mar 18;17(3):723–742. doi: 10.1080/15548627.2020.1731266

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© 2020 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 5. — PAK1-induced phosphorylation on T101 of ATG5 inhibits ATG5 ubiquitination and promotes its stability. (A) The levels of ATG5 mRNA in U87 cells or LN229 cells with indicated treatment were measured using qRT-PCR. (B and C) The effect of treatment of CHX (20 μg/ml) on the half-life of ATG5 protein in LN229 or U87 cells with indicated treatment, respectively. (D) The effect of MG-132 on ATG5 degradation in LN229 cells with PAK1 deficiency. (E) The effect of different ATG5 constructs on the levels of ATG5 protein in HEK293 T cells and LN229 cells, respectively. (F) The effect of ATG5 (T75) mutants on the expression of ATG5 protein. (G) The effect of CHX treatment on the levels of ATG5 protein in HEK293 T cells transfected with different ATG5 plasmids. (H) The effect of different ATG5 plasmids on the level of ATG5 ubiquitination in HEK293 T cells. We used an anti-Flag antibody to check the protein level of ATG5 in E-H.