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. 2023 Jul 8;14(7):408. doi: 10.1038/s41419-023-05938-2

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© The Author(s) 2023

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 4 — A LPP protein levels in different groups of BCa cells after treatment with MG132 (10 μM, 12 h) or DMSO. The total (B, C) and K11-linked (D, E) ubiquitination levels of LPP in UBE2S-knockdown or TRIM21-knockdown HEK293T cells transfected with corresponding plasmids (48 h) and treated with MG132 (10 μM, 12 h). WT wild type. The total (F) and K11-linked (G) ubiquitination levels of LPP in UBE2S- and TRIM21-overexpressing HEK293T cells transfected with corresponding plasmids (48 h) and treated with MG132 (10 μM, 12 h). H An in vitro ubiquitination assay was performed in the presence of LPP, ubiquitin (Ub), Ub-K11R, UBE1, UBE2S and TRIM21. The reaction was analyzed by western blotting with an anti-LPP antibody (25045-1-AP, Proteintech). I Schematic diagram of TRIM21 and its truncated mutant. The total (J) and K11-linked (K) ubiquitination levels of LPP in full-length TRIM21 and TRIM21-ΔRING HEK293T cells transfected with the corresponding plasmids (48 h) and treated with MG132 (10 μM, 12 h).