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. 2022 Jul 19;10:922675. doi: 10.3389/fcell.2022.922675

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Copyright © 2022 Liu, Cao, Hu, Ye, Tian and He.

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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TRIM28 breaks the interaction between MAGE-C2 and MDM2 to promote p53 ubiquitination. (A) GST pulldown assay was used to validate the interaction relationship between TRIM28, MAGE-C2, and MDM2. MDM2 first bound to GST–MAGE-C2 on GST beads, and then TRIM28 was gradiently added. Beads with samples were immunoblotted with the MDM2 antibodies. (B) In vitro ubiquitination assay. His-ubiquitin, ubiquitin E1, UbcH5B E2, Mg-ATP, GST-p53, and the indicated MAGE-C2, MDM2, and TRIM28 proteins were incubated for specific time at 37°C and detected by using anti-p53 immunoblotting. (C) Ubiquitination assay in cells. HEK293T cells were transfected with HA-ubiquitin and the indicated plasmids. The level of p53 ubiquitination was determined by using anti-Flag M2-agarose redbeads purification and anti-HA Western blot.