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. 2021 Jan 22;12(1):118. doi: 10.1038/s41419-021-03398-0

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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. 5 — A Interaction of endogenous CSN6 with endogenous UBR5. Equal amounts of cell lysates from A375 and MV3 cells overexpressing CSN6 were immunoprecipitated with the indicated antibodies and immunoblotted with anti-Flag or anti-UBR5 antibodies. B Total cellular extracts from 293FT cells transfected with increasing amounts of CSN6 plasmids were prepared and subjected to western blotting using the indicated antibody. C Total cell lysates from CSN6-knockdown and CSN6-rescued CSN6-knockdown A375 and MV3 cells were prepared and subjected to western blotting with the indicated antibody. D The UBR5 turnover rate of CSN6-knockdown cells was determined. CSN6-knockdown A375 and MV3 cells were treated with CHX for the indicated times. Cell lysates were immunoblotted with the indicated antibodies (left). The turnover of UBR5 is indicated graphically (right). E Cell lysates were prepared from A375 and MV3 cells expressing Flag-tagged CSN6 that had been treated with or without MG132 for 8 h. Equal amounts of cell lysates were immunoblotted with the indicated antibodies. F, G A375, MV3 and 293FT cells transfected with the indicated plasmids were treated with MG132 for 8 h before harvest. Ubiquitinated UBR5 and CDK9 proteins were immunoprecipitated with an anti-HA antibody and immunoblotted with anti-CDK9 and anti-UBR5 antibodies.