SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways

• Published in: Molecular cell Vol. 50; no. 6; pp. 919 - 930
• Main Authors: Park, Jeongsoon, Chen, Yue, Tishkoff, Daniel X., Peng, Chao, Tan, Minjia, Dai, Lunzhai, Xie, Zhongyu, Zhang, Yi, Zwaans, Bernadette M.M., Skinner, Mary E., Lombard, David B., Zhao, Yingming
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 27.06.2013
• Subjects: Acetylation; Amino Acid Sequence; Animals; Cell Respiration; Cells, Cultured; Consensus Sequence; fatty acid metabolism; Glycosylation; Kinetics; lysine; Lysine - metabolism; mammals; Metabolic Networks and Pathways; Mice; Mice, Knockout; Mitochondria - enzymology; Molecular Sequence Annotation; nuclear proteins; post-translational modification; Protein Interaction Maps; Protein Processing, Post-Translational; Protein Transport; proteins; Proteome - metabolism; pyruvate dehydrogenase (lipoamide); Pyruvate Dehydrogenase Complex - metabolism; Sirtuins - genetics; Sirtuins - metabolism; succinate dehydrogenase (quinone); Succinate Dehydrogenase - metabolism; tricarboxylic acid cycle

Protein function is regulated by diverse posttranslational modifications. The mitochondrial sirtuin SIRT5 removes malonyl and succinyl moieties from target lysines. The spectrum of protein substrates subject to these modifications is unknown. We report systematic profiling of the mammalian succinylo...