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. 2019 Sep 4;10:3987. doi: 10.1038/s41467-019-11773-x

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© The Author(s) 2019

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 — Poly-SUMOylation does not lead to destabilization of CCAN proteins. a U2OS cells stably expressing His10-SUMO2 were infected with lentiviruses encoding shRNAs against SENP6 or a nontargeting control shRNA (ctrl shRNA) 3 days prior to lysis. Where indicated, cells were treated with 10 µM MG132 for 4 h prior to lysis. Cells were lysed and SUMOylated proteins were enriched by means of Ni-NTA pulldown. Inputs and His10-pulldown elutions were analysed by immunoblotting with the indicated antibodies. Equal loading was verified by Ponceau S staining. b U2OS cells stably expressing His10-ubiquitin were infected with lentiviruses encoding shRNAs against SENP6 or a nontargeting control shRNA (ctrl shRNA) 3 days prior to lysis. Where indicated cells were treated with 10 µM MG132 for 4 h prior to lysis. Cells were lysed and ubiquitinated proteins were enriched by means of Ni-NTA pulldown. Inputs and His10-pulldown elutions were analysed by immunoblotting with the indicated antibodies. Equal loading was verified by Ponceau S staining. Source data are provided as a Source Data file