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The First Identification of Lysine Malonylation Substrates and Its Regulatory Enzyme
文献类型：期刊论文
| 作者 | Peng, Chao1; Lu, Zhike1; Xie, Zhongyu1; Cheng, Zhongyi1; Chen, Yue1; Tan, Minjia1 ; Luo, Hao1; Zhang, Yi6; He, Wendy5; Yang, Ke4
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| 刊名 | MOLECULAR & CELLULAR PROTEOMICS
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| 出版日期 | 2011-12 |
| 卷号 | 10期号:12 |
| ISSN号 | 1535-9476 |
| DOI | 10.1074/mcp.M111.012658 |
| 文献子类 | Article |
| 英文摘要 | Protein post-translational modifications (PTMs) at the lysine residue, such as lysine methylation, acetylation, and ubiquitination, are diverse, abundant, and dynamic. They play a key role in the regulation of diverse cellular physiology. Here we report discovery of a new type of lysine PTM, lysine malonylation (Kmal). Kmal was initially detected by mass spectrometry and protein sequence-database searching. The modification was comprehensively validated by Western blot, tandem MS, and high-performance liquid chromatography of synthetic peptides, isotopic labeling, and identification of multiple Kmal substrate proteins. Kmal is a dynamic and evolutionarily conserved PTM observed in mammalian cells and bacterial cells. In addition, we demonstrate that Sirt5, a member of the class III lysine deacetylases, can catalyze lysine demalonylation and lysine desuccinylation reactions both in vitro and in vivo. This result suggests the possibility of nondeacetylation activity of other class III lysine deacetylases, especially those without obvious acetylation protein substrates. Our results therefore reveal a new type of PTM pathway and identify the first enzyme that can regulate lysine malonylation and lysine succinylation status. Molecular & Cellular Proteomics 10: 10.1074/mcp.M111.012658, 1-12, 2011. |
| WOS关键词 | PROTEIN POSTTRANSLATIONAL MODIFICATIONS ; MASS-SPECTROMETRY ; SEQUENCE DATABASES ; COENZYME-A ; ACETYLATION ; PHOSPHOPEPTIDES ; OBESITY ; COA |
| 资助项目 | National Institutes of Health[00000000] ; National Institute on Aging[T32-AG000114] ; Ellison Medical Foundation[AG-NS-0583-09] ; Elsa U. Pardee Foundation[00000000] ; American Foundation for Aging Research[00000000] ; University of Michigan Comprehensive Care Center[00000000] |
| WOS研究方向 | Biochemistry & Molecular Biology |
| 语种 | 英语 |
| WOS记录号 | WOS:000298290300028 |
| 出版者 | AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC |
| 源URL | [http://119.78.100.183/handle/2S10ELR8/278323]  |
| 专题 | 天然药物化学研究室 |
| 通讯作者 | Zhao, Yingming |
| 作者单位 | 1.Univ Chicago, Ben May Dept Canc Res, Chicago, IL 60637 USA; 2.Tsinghua Univ, Sch Life Sci, Beijing 100084, Peoples R China 3.Dept Pathol, Ann Arbor, MI 48109 USA; 4.Univ Chicago, Dept Surg, Mol Oncol Lab, Chicago, IL 60637 USA; 5.Gladstone Inst Virol & Immunol, San Francisco, CA 94158 USA; 6.Chinese Acad Sci, Shanghai Inst Mat Med, Shanghai 201203, Peoples R China; 7.Univ Michigan, Inst Gerontol, Ann Arbor, MI 48109 USA; |
| 推荐引用方式 GB/T 7714 | Peng, Chao,Lu, Zhike,Xie, Zhongyu,et al. The First Identification of Lysine Malonylation Substrates and Its Regulatory Enzyme[J]. MOLECULAR & CELLULAR PROTEOMICS,2011,10(12). |
| APA | Peng, Chao.,Lu, Zhike.,Xie, Zhongyu.,Cheng, Zhongyi.,Chen, Yue.,...&Zhao, Yingming.(2011).The First Identification of Lysine Malonylation Substrates and Its Regulatory Enzyme.MOLECULAR & CELLULAR PROTEOMICS,10(12). |
| MLA | Peng, Chao,et al."The First Identification of Lysine Malonylation Substrates and Its Regulatory Enzyme".MOLECULAR & CELLULAR PROTEOMICS 10.12(2011). |
入库方式： OAI收割
来源：上海药物研究所
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