STAT3 Undergoes Acetylation-dependent Mitochondrial Translocation to Regulate Pyruvate Metabolism

• DOI: 10.1038/srep39517
• Publication Date: 2016-12-22T10:37:22Z
• Authors: Yan S. Xu; Jinyuan J. Liang; Yumei Wang; Xiang-zhong J. Zhao; Li Xu; Ye-yang Xu; Quanli C. Zou; Junxun M. Zhang; Cheng-e Tu; Yan-ge Cui; Wei-hong Sun; Chao Huang; Jing-hua Yang; Y. Eugene Chin
• Keywords: Cell Nucleus; Membrane Potential, Mitochondrial; Cytoplasm; 0303 health sciences; Citric Acid Cycle; Acetylation; Pyruvate Dehydrogenase Complex; Fibroblasts; Article; Mitochondria; Mice; Protein Transport; 03 medical and health sciences; HEK293 Cells; A549 Cells; Acetyl Coenzyme A; Cell Line, Tumor; Animals; Humans; Insulin; Oxidation-Reduction; Protein Processing, Post-Translational; HeLa Cells

Cytoplasmic STAT3, after activation by growth factors, translocates to different subcellular compartments, including nuclei and mitochondria, where it carries out biological functions. However, the precise mechanism which STAT3 undergoes mitochondrial translocation subsequently regulates tricarboxylic acid (TCA) cycle-electron transport chain (ETC) remains poorly understood. Here, we clarify this process visualizing acetylation in starved cells serum reintroduction or insulin stimulation. CBP-acetylated response introduction In associates with pyruvate dehydrogenase complex E1 (PDC-E1) accelerates conversion of acetyl-CoA, elevates membrane potential, promotes ATP synthesis. SIRT5 deacetylates thereby inhibiting its function metabolism. A549 lung cancer cell line, constitutively acetylated localizes maintains potential synthesis an active state.