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. 2022 Dec 10;13:7658. doi: 10.1038/s41467-022-35424-w

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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. 5 — a LC-MS/MS analysis identified Sirt6 deacetylated K163 on Stat5. Lysates from human chondrocytes with or without Sirt6 treatment. b Interaction model between Stat5 and Sirt6. c Conservation of Stat5 K163 in different species. d K163 is located in exon 5 of STAT5, which was mutated to arginine through “A” replaced by “G”. The surface from molecular simulation showed the mutant site (K163R). e Sirt6 deacetylated Stat5 via K163. The acetylation level of WT Stat5 with Sirt6 treatment was analyzed by western blot. n = 3 independent biological replicates per group. f, g Human chondrocytes were transfected with WT Stat5 or mutant Stat5, followed by IL-15 treatment. The phosphorylation of Stat5 and the cellular localization of Stat5 was determined by western blot. n = 3 independent biological replicates per group (f). Immunofluorescent staining of Stat5. n = 3 independent biological replicates per group (g). h Transcriptional activity of WT and mutant Stat5. Human chondrocytes were co-transfected with WT Stat5 or mutant Stat5, followed by IL-15 treatment. n = 6 independent biological replicates per group. i, j K163 of Stat5 is required for Sirt6-regulated IL-15/JAK3/STAT5 signaling pathway. After IL-15 treatment, the phosphorylation of Stat5 and the cellular localization of Stat5 were analyzed. n = 3 independent biological replicates per group (i). Immunofluorescent staining of Stat5. n = 3 independent biological replicates per group (j). k The transcriptional activity of WT and mutant Stat5 in human chondrocytes transfected by pcDNA3.1 or pcDNA3.1-Sirt6, followed by IL-15 treatment. n = 6 independent biological replicates per group. l Molecular model for dysregulated Sirt6 in chondrocyte senescence and OA pathogenesis. Scar bar: g, j 20 μm. Data were presented as the mean ± s.e.m. P values are from two-tailed unpaired Student’s t-test (h, k). Source data are provided as a Source Data file.