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. 2022 Aug 10;13(8):698. doi: 10.1038/s41419-022-05136-6

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© The Author(s) 2022

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. 3 — A Schematic diagram of wild-type ubiquitin and its mutant constructs (M1, K6, K11, K27, K29, K33, K48, and K63). B Ubiquitination assay of Raf-1 was performed in HEK293T cells transfected with Flag-Raf-1 and HA-Ub and treated with a proteasome inhibitor MG132. C HEK293T cells were transfected with Flag-Raf-1 and each HA-Ub mutant (K6, K11, K29, K33, and K48) and treated with a proteasome inhibitor MG132. And then ubiquitination assay of Raf-1 was performed for checking the association between the specific lysine sites of polyubiquitination and UPS. D Myc-USP7 and Flag-Raf-1 were transfected into HEK293T cells and Flag-Raf-1 was precipitated for deubiquitination assay. For checking the decrease of overall polyubiquitination of Raf-1 by DUB activity of USP7, deubiquitination assay was performed. E HEK293T cells were transfected with each HA-Ub mutant (M1, K6, K11, K27, K33, and K48) and Myc-USP7. A change in the polyubiquitin chains (M1, K6, K11, K27, K33, and K48) of Raf-1 by USP7 was detected through deubiquitination assay.