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. 2022 Dec 12;13:7439. doi: 10.1038/s41467-022-35219-z

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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. 8 — a The effect of SIRT7 overexpression on IMP2 acetylation. HEK293T cells were transfected with the indicated expression plasmid, and IMP2 acetylation was assessed by IP and WB (left panel). Quantification of the acetylated IMP2 relative to IMP2 (n = 3) (right panel). p = 0.0174. b The effect of Sirt7 deficiency on IMP2 acetylation. Protein lysates of iBAT were subjected to IP, after which the acetylated IMP2 was detected by WB (left panel). Quantification of the acetylated IMP2 relative to IMP2 (n = 3) (right panel). p = 0.0170. c Mapping of the region of the interaction between IMP2 and SIRT7. Halo-SIRT7 pull-down assay with lysates of HEK293T cells expressing the indicated IMP2 deletion mutants fused with GAL4DBD. See also Supplementary Fig. 6a. d The effect of SIRT7 overexpression on IMP2^K438R and IMP2^K439R acetylation. HEK293T cells were transfected with the indicated expression plasmid, and IMP2 acetylation was assessed by IP and WB. Quantification of the acetylated IMP2 is shown in Supplementary Fig. 6b. e Binding between in vitro-transcribed long Ucp1 3′-UTR and IMP2 (IMP2^WT, IMP2^K438R, IMP2^K438Q) (n = 4 independent samples per group). p = 0.0401 (IMP2^WT vs. IMP2^K438Q), p = 1.7E-05 (IMP2^K438R vs. IMP2^K438R). f The effect of IMP2 mutant on the translation of luciferase-Ucp1 UTR fusion mRNA. luciferase-Ucp1 UTR mRNA was transcribed in vitro and used in an insect cell-free translation system with recombinant protein in E. coli for IMP2^WT, IMP2^K438R, and IMP2^K438Q (n = 3 independent samples per group). Translation was estimated by the gain in luciferase activity after incubation for 5 h at 25 °C. p = 0.0016 (Control vs. IMP2^WT), p = 0.0106 (Control vs. IMP2^K438R). g Proposed model for the suppression of brown fat thermogenesis through attenuation of Ucp1 mRNA translation via SIRT7-dependent deacetylation of IMP2. See Discussion for details. WB western blotting, IP immunoprecipitation, N.S. not significant. Data are presented as means ± SEM. All numbers (n) are biologically independent samples. *p < 0.05, **p < 0.01 by two-tailed Student’s t-test. Source data are provided as a Source Data file.