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. 2024 May 29;22:122. doi: 10.1186/s12915-024-01901-5

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© The Author(s) 2024

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 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. 3 — The PP6 complex negatively regulates inhibitory phosphorylation of RIPK1 to drive PANoptosis. A Immunoblots for S166 and S321 phospho-RIPK1 (pRIPK1) and total RIPK1 (tRIPK1) using cell lysates and immunoblots for high mobility group box 1 (HMGB1) and lactate dehydrogenase (LDH) using culture supernatants from bone marrow-derived macrophages (BMDMs) treated with TAK1 inhibitor (TAK1i) for 8 h. Blots were re-probed for β-ACTIN to serve as the internal loading control. The blots presented are representative of three independent experiments. NT: non-targeting siRNA; Ppp6r1+r2+r3: BMDMs treated with siRNAs against Ppp6r1, Ppp6r2, and Ppp6r3. B Schematic illustrating the potential mechanism for the PP6 complex to drive TAK1i-induced, RIPK1-dependent PANoptosis in BMDMs. The phosphorylation (P) marks denote the RIPK1 S166 (red, spiked) and S321 (green, rounded) phosphorylations