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. 2020 Aug 14;39:158. doi: 10.1186/s13046-020-01658-z

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© The Author(s) 2020

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. 6 — TNFAIP8 promotes ERK activation by interacting with its upstream factor Rac1. a, b The interaction of TNFAIP8 and Rac1 was assessed by co-immunoprecipitation experiments in 293 T cells and AML cells, K562 and HL60. Immunoprecipitates were generated by anti-Flag antibody and TNFAIP8-bound Rac1 was detected by immunoblotting with anti-Rac1 antibody. c The effect of TNFAIP8 on Rac1 activation. The levels of Rac1-GTP were determined by a PAK-GST pull-down assay in K562, HL60 cells transduced with Flag-tagged TNFAIP8 or control vector, and corresponding resistant cell lines K562/A02 and HL60/ADR transduced with shTNFAIP8 or shNC which were all stimulated with ADM for 4 h. d Rac1 inhibition by EHOP-016 (5 μM, 12 h) attenuated the positive effect of TNFAIP8 overexpression on ERK phosphorylation