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. 2022 May 18;13(5):466. doi: 10.1038/s41419-022-04918-2

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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. 1 — A Increased MIF acetylation in cells treated with HDAC inhibitors. HEK293T cells were transfected with MIF-Myc and treated with nicotinamide (NAM) or trichostatin A (TSA). MIF protein was immunoprecipitated with anti-Myc antibody and probed with anti-Ac-K antibody to reveal acetylated MIF protein. B Quantification of MIF acetylation showed in A. Data shown were independent points and mean; one-way ANOVA; n = 3; ***p < 0.001. C Increased MIF acetylation in tubastatin A-treated cells. HEK293T cells were transfected with MIF-Myc and treated with HDAC6 inhibitor tubastatin A at indicated concentrations. MIF protein was immunoprecipitated with anti-Myc antibody and probed with anti-Ac-K antibody. D Quantification of MIF acetylation showed in C. Data shown were independent points and mean; one-way ANOVA; n = 4; **p < 0.01. E Decreased MIF acetylation in HDAC6-overexpressing cells. HEK293T cells were transfected with MIF-Myc with or without HDAC6-Flag. MIF protein was immunoprecipitated with anti-Myc antibody and probed with anti-Ac-K antibody. F Quantification of MIF acetylation showed in E. Data shown were independent points and mean; paired t-test; n = 3; **p < 0.01. G Increased MIF acetylation in HDAC6 mutant mice. The lysates from WT and HDAC6 mutant cortex were immunoprecipitated with anti-MIF antibody and probed with anti-Ac-K antibody. H Quantification of MIF acetylation showed in G. Data shown were independent points and mean; paired t-test; n = 3; *p < 0.05. I The second deacetylase domain of HDAC6 is required for MIF deacetylation. HDAC6-Flag, two deacetylase domain mutants (H216A and H611A), and MIF-Myc were transfected into HEK293T cells. MIF was immunoprecipitated with anti-Myc antibody and probed with anti-Ac-K antibody. J Quantification of MIF acetylation showed in I. Data shown were independent points and mean; one-way ANOVA; n = 3; *p < 0.05. K K78 of MIF is the major acetylation site. MIF-Myc, K33R-Myc, K67R-Myc, and K78R-Myc were transfected into HEK293T cells. MIF was immunoprecipitated with anti-Myc antibody and probed with anti-Ac-K antibody. L Quantification of MIF acetylation is shown in K. Data shown were independent points and mean; one-way ANOVA; n = 3; F = 27.39, p < 0.001; ***p < 0.001.