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. 2019 Jul 15;9:10245. doi: 10.1038/s41598-019-46526-9

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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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Perturbation of the ubiquitin proteome in macrophages results in accumulation of high-molecular weight ubiquitinated proteins. (A) Immunoblots of RAW264.7 whole cell lysates following treatment with DUB^inh (3.5 µM, 1 h), EerI (10 µM, 1 h) or MG132 (5 µM, 2 h) probed with specific antibodies for total mono- and poly-ubiquitinated proteins, K63-, K48- or linear M1-linked specific polyubiquitin chains and β-actin. The asterisk represents the free monoubiquitin. (B) RAW264.7 whole cell lysates were incubated with DUB^inh-Biotin or ΔCN-biotin before immunoprecipitation using streptavidin-coated beads. The retained proteins were immunoblotted with antibodies for MYSM1 (95 kDa), DUBA (61 kDa), Ataxin3 (42 kDa), USP14 (60 kDa), UCH37 (37 kDa), Rpn11 (35 kDa), YOD1 (37 kDa) and USP25 (126 kDa). Data are representative of three independent experiments. Full-length immunoblots are presented in Supplementary Figs S6 and S7.