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. 2022 Nov 16;41:323. doi: 10.1186/s13046-022-02526-8

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© The Author(s) 2022

Open AccessThis 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 licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by/4.0/. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated in a credit line to the data.

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Fig. 5 — ARPC1B disrupted the TRIM21-mediated IFI16 and HuR ubiquitylation and degradation. A, B Co-IP assays were performed with an anti-HA antibody on cell lysates from HEK293 cells transfected with Flag-ARPC1B alone or together with the indicated HA-IFI16 (A) or HA-HuR (B) constructs. The upper panel is a schematic representation of wild-type sequences and the indicated deletion mutants. C Western blot analysis of co-IPs in lysates of HEK293 cells transfected with the indicated Flag-ARPC1B constructs together with HA-IFI16 (left panel) or HA-HuR (right panel). The upper panel is a schematic representation of wild-type ARPC1B and the two indicated mutants. D, E Co-IP analysis revealing the impact of ARPC1B knockdown (D) or ARPC1B overexpression (E) on the interaction between TRIM21 and IFI16 or TRIM21 and HuR