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. 2019 Mar 11;47(9):4476–4494. doi: 10.1093/nar/gkz163

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© The Author(s) 2019. Published by Oxford University Press on behalf of Nucleic Acids Research.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 9. — Fbxw7α interacts with phosphorylated IRF1 via T181. (A) Co-immunoprecipitation of HA-Fbxw7α in extracts of HEK293 cells, and western blots using anti-HA antibody to detect associated FLAG-IRF1. Cells were treated with MG132 for 6 h prior to lysis. Blots were re-probed with anti-HA to determine IP efficiency n.s. = non-specific band is indicated. (B) Co-IP experiment as in (A) but with anti-FLAG antibody to IP and western blot with anti-HA to detect complex formation with HA-Fbxw7α or a mutant lacking the WD40 domain (HA-Fbxw7α ΔWD40). (C) HA-Fbxw7α, GSK3β-HA and FLAG-IRF1 were co-expressed in HEK293 for 48 h, 6 h prior to lysis cells were treated with 10 μM MG132. Lysates were immunoprecipitated with anti-FLAG and probed with anti-HA to detect Fbxw7α interaction. The blots were also probed with the anti-pT/S antibody and FLAG to determine relative levels of IRF1 phosphorylation. (D) Immunoprecipitations as for (B) but with the inclusion of IRF1 T181A, S185A, T181A/S185A and T181D mutants.