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. 2021 Apr 6;12:2043. doi: 10.1038/s41467-021-22319-5

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© The Author(s) 2021

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 Co-IP confirming endogenous FBW7 interaction with TRIP12 and vice versa in HEK293T cells, black star (*) represents a nonspecific band of unknown identity. b Schematic for experiments in c and d. c In vitro 35S-FBW7α ubiquitylation experiment in the presence of the indicated reagents. d In vitro deubiquitylation of 35S-FBW7α by USP2. e Schematic of in vitro translated 35S-FBW7 pulldown with MYC-TRIP12 from HEK293T cells. f Autoradiograph showing MYC-TRIP12 interaction with ubiquitylated FBW7. g Western blots showing the interaction of MYC-FBW7 with FLAG-TRIP12 in HCT116 cells pre-treated for 24 h with either NAE1 inhibitor (MLN4924) or DMSO as control. h Schematic of GFP-TRIP12 deletion mutants. i Western blots showing the interaction of MYC-FBW7 with GFP-TRIP12, GFP-TRIP12^ΔHECT, GFP-TRIP12^{ΔHECT/ ΔWWE} mutants in HCT116 cells, black star (*) represents a nonspecific band of unknown identity. All blots are representative of at least three independent experiments. See also Supplementary Fig. 4. Source data are provided as a Source Data file.