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. 2022 Dec 6;20:571. doi: 10.1186/s12967-022-03782-0

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© The Author(s) 2022

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. 2 — GCN5L1 acetylated TFAM at K76 site. A The heatmap of mass spectrometry-based acetylated proteomics. B–E Acetylation level of TFAM was detected by immunoprecipitation in GCN5L1 overexpression or knockdown TECs. F–I Acetylation level of TFAM was detected in GCN5L1 overexpression or knockdown TECs visualized by Duolink proximity ligation assay. J The co-localization of TFAM with GCN5L1 was detected by immunofluorescent staining. K Diagram for TFAM potential acetylation sites and the construction of mutants. L, M Acetylation level of TFAM was detected by immunoprecipitation in TECs co-transfected with GCN5L1 and TFAM site mutation overexpressing plasmids. N The structure model of GCN5L1 interaction with TFAM. ns: not significant, *P < 0.05, and **P < 0.01