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. 2021 May 5;28(10):2888–2899. doi: 10.1038/s41418-021-00790-3

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© The Author(s), under exclusive licence to ADMC Associazione Differenziamento e Morte Cellulare 2021

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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Fig. 1 — a FLAG-tagged RIP3 was transfected into HeLa and HEK293T cells, followed by immunoprecipitation with the RIP3 antibody and immunoblotting analysis with TRIM25 and RIP3 antibodies, respectively. b Immunoprecipitation analysis with TRIM25 or RIP3 antibodies in HT-29 cells. c Co-immunoprecipitation analysis of RIP3 and TRIM25 by treatment with TNF/Z-VAD/Smac-mimetic (TSZ) stimuli for indicated hours in HT-29 cells. d RIP3 colocalized with TRIM25 in the cytoplasm of HT-29 cells. Endogenous RIP3 and TRIM25 were stained by anti-RIP3 (red) and anti-TRIM25 (green) antibodies, respectively. Scale bar, 10 µm. e Schematic of TRIM25 and different truncations. f His-tagged TRIM25 or its mutants and GFP-tagged RIP3 were co-transfected into HeLa cells. The cell lysates were immunoprecipitated with an anti-His antibody and then immunoblotted with the indicated antibodies. g HT-29 cells were primed with TSZ for 6 h, followed by immunoprecipitation with anti-TRIM25 antibody and probed with the indicated antibodies. h Schematic of RIP3 and different truncations. i GFP-tagged RIP3 or its mutants were transfected into HEK293T cells. The cell lysates were immunoprecipitated with an anti-GFP antibody and then immunoblotted with the indicated antibodies.