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. 2022 Jun 13;13(6):548. doi: 10.1038/s41419-022-04997-1

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© The Author(s) 2022

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. 4 — A SDS-PAGE silver staining showed typical pull-down results of Acsl4 after incubation with PL1 cell lysate. Mass spectrometry identified the band framed in the oval as Hsp90. B The interaction between Acsl4, Drp1, and Hsp90 was confirmed by co-immunoprecipitation in PL1 and PG7 cells. C Confocal images showed colocalization of Acsl4 (red) and Hsp90 (green), Drp1 (red), and Hsp90 (green) in PL1 and PG7 cells. Nuclei were counterstained with Hoechst (blue). Scale bars: 10 μm. D Expression levels of proteins in Hsp90-Acsl4 pathway were determined by western blot in the indicated groups. Data indicated as mean ± S.D. (n = 5 experiments). E, F Thermal stabilization of Acsl4 in PL1 and PG7 cells of indicated groups was determined following standard cellular thermal shift protocol with heat treatment from 37 °C to 65 °C. (PL1 cells: erastin 1 μm, PG7 cells: erastin 2 μm). Data indicated as mean ± S.D. (n = 3 experiments). *p < 0.05, **p < 0.01, ***p < 0.001.