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. 2018 Sep 7;8:13418. doi: 10.1038/s41598-018-31734-6

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© The Author(s) 2018

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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USP4 targets TRAF6 through its USP domain. (A) HEK293T cells transfected with either HA-USP4 or a control vector for 48 h were lysed and immunoprecipitated with anti-HA agarose beads. This was followed by western blot analysis of eluted immunocomplexes with TRAF6. (B,D) HEK293T cells transfected with Flag-TRAF6, together with either HA-USP4, mutated HA-USP4 (CA) or an empty vector were collected 48 h post-transfection and immunoprecipitated with either anti-HA agarose beads (B) or anti-Flag agarose beads (D). (C) USP4 wild-type (WT) contains a DUSP domain and a C-terminal USP domain. N260 lacks the C-terminal USP domain, C261 lacks the DUSP domain. (E) Lysates from HEK293T cells co-transfected with Flag-TRAF6 and either full-length HA-USP4 (WT) or its truncated constructs (N or C), and then were subjected to immunoprecipitation with anti-Flag agarose beads followed by SDS-PAGE analysis with anti-HA-HRP antibody). The independent experiments were performed in triplicate. Please note the mutated HA-USP4 (CA) expression construct was generated using site-directed mutagenesis(G-C).