Sirtuin 1/sirtuin 3 are robust lysine delactylases and sirtuin 1-mediated delactylation regulates glycolysis
文献类型：期刊论文
| 作者 | Du, Runhua4,5; Gao, Yanmei3; Yan, Cong4; Ren, Xuelian4,5; Qi, Shankang4; Liu, Guobin4; Guo, Xinlong4; Song, Xiaohan4; Wang, Hanmin4; Rao, Jingxin2 |
| 刊名 | ISCIENCE
 |
| 出版日期 | 2024-10-18 |
| 卷号 | 27期号:10页码:23 |
| DOI | 10.1016/j.isci.2024.110911 |
| 通讯作者 | Huang, He(hhuang@simm.ac.cn) |
| 英文摘要 | Lysine lactylation (Kla), an epigenetic mark triggered by lactate during glycolysis, including the Warburg effect, bridges metabolism and gene regulation. Enzymes such as p300 and HDAC1/3 have been pivotal in deciphering the regulatory dynamics of Kla, though questions about additional regulatory enzymes, their specific Kla substrates, and the underlying functional mechanisms persist. Here, we identify SIRT1 and SIRT3 as key "erasers" of Kla, shedding light on their selective regulation of both histone and nonhistone proteins. Proteomic analysis in SIRT1/SIRT3 knockout HepG2 cells reveals distinct substrate specificities toward Kla, highlighting their unique roles in cellular signaling. Notably, we highlight the role of specific Kla modifications, such as those on the M2 splice isoform of pyruvate kinase (PKM2), in modulating metabolic pathways and cell proliferation, thereby expanding Kla's recognized functions beyond epigenetics. Therefore, this study deepens our understanding of Kla's functional mechanisms and broadens its biological significance. |
| WOS关键词 | PYRUVATE-KINASE M2 ; PROTEIN ; CANCER ; PURIFICATION ; ACETYLATION ; DEACETYLASE ; BINDING |
| 资助项目 | National Natural Science Foundation of China[22277125] ; National Natural Science Foundation of China[92253306] ; Natural Science Foundation of Shanghai[23ZR1474600] ; Shanghai Municipal Science and Technology Major Project |
| WOS研究方向 | Science & Technology - Other Topics |
| 语种 | 英语 |
| WOS记录号 | WOS:001319902400001 |
| 出版者 | CELL PRESS |
| 源URL | [http://119.78.100.183/handle/2S10ELR8/313642]  |
| 专题 | 中国科学院上海药物研究所 |
| 通讯作者 | Huang, He |
| 作者单位 | 1.Lingang Lab, Shanghai 201203, Peoples R China 2.Chinese Acad Sci, Shanghai Inst Mat Med, State Key Lab Drug Discovery, Shanghai 201203, Peoples R China 3.Nanjing Univ Chinese Med, Sch Chinese Mat Med, Nanjing 210023, Peoples R China 4.Chinese Acad Sci, Shanghai Inst Mat Med, State Key Lab Chem Biol, Shanghai 201203, Peoples R China 5.Univ Chinese Acad Sci, Hangzhou Inst Adv Study, Sch Pharmaceut Sci & Technol, Hangzhou 310024, Peoples R China |
| 推荐引用方式 GB/T 7714 | Du, Runhua,Gao, Yanmei,Yan, Cong,et al. Sirtuin 1/sirtuin 3 are robust lysine delactylases and sirtuin 1-mediated delactylation regulates glycolysis[J]. ISCIENCE,2024,27(10):23. |
| APA | Du, Runhua.,Gao, Yanmei.,Yan, Cong.,Ren, Xuelian.,Qi, Shankang.,...&Huang, He.(2024).Sirtuin 1/sirtuin 3 are robust lysine delactylases and sirtuin 1-mediated delactylation regulates glycolysis.ISCIENCE,27(10),23. |
| MLA | Du, Runhua,et al."Sirtuin 1/sirtuin 3 are robust lysine delactylases and sirtuin 1-mediated delactylation regulates glycolysis".ISCIENCE 27.10(2024):23. |
入库方式： OAI收割
来源：上海药物研究所
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