HDAC1/2/3 are major histone desuccinylases critical for promoter desuccinylation
文献类型：期刊论文
| 作者 | Li, Jialun1; Lu, Lu2,3; Liu, Lingling4; Ren, Xuelian5; Chen, Jiwei6; Yin, Xingzhi2,3; Xiao, Yanhui2,3; Li, Jiwen2,3; Wei, Gang4; Huang, He5 |
| 刊名 | CELL DISCOVERY
 |
| 出版日期 | 2023-08-15 |
| 卷号 | 9期号:1页码:17 |
| DOI | 10.1038/s41421-023-00573-9 |
| 通讯作者 | Huang, He(hhuang@simm.ac.cn) ; Wei, Wei(weiwei050922@163.com) ; Wong, Jiemin(jmweng@bio.ecnu.edu.cn) |
| 英文摘要 | Lysine succinylation is one of the major post-translational modifications occurring on histones and is believed to have significant roles in regulating chromatin structure and function. Currently, histone desuccinylation is widely believed to be catalyzed by members of the SIRT family deacetylases. Here, we report that histone desuccinylation is in fact primarily catalyzed by the class I HDAC1/2/3. Inhibition or depletion of HDAC1/2/3 resulted in a marked increase of global histone succinylation, whereas ectopic expression of HDAC1/2/3 but not their deacetylase inactive mutants downregulated global histone succinylation. We demonstrated that the class I HDAC1/2/3 complexes have robust histone desuccinylase activity in vitro. Genomic landscape analysis revealed that histone succinylation is highly enriched at gene promoters and inhibition of HDAC activity results in marked elevation of promoter histone succinylation. Furthermore, our integrated analysis revealed that promoter histone succinylation positively correlates with gene transcriptional activity. Collectively, we demonstrate that the class I HDAC1/2/3 but not the SIRT family proteins are the major histone desuccinylases particularly important for promoter histone desuccinylation. Our study thus sheds new light on the role of histone succinylation in transcriptional regulation. |
| WOS关键词 | LYSINE SUCCINYLATION ; GENE-EXPRESSION ; DEACETYLASE ; COMPLEX ; SIRT5 ; PROTEINS ; SMRT ; MALONYLATION ; ACETYLATION ; METABOLISM |
| 资助项目 | National Natural Science Foundation of China[32130051] ; National Natural Science Foundation of China[82173073] ; Science and Technology Commission of Shanghai Municipality[20JC1411500] ; ECNU Public Platform for Innovation[011] ; Instruments Sharing Platform of the School of Life Sciences, East China Normal University |
| WOS研究方向 | Cell Biology |
| 语种 | 英语 |
| 出版者 | SPRINGERNATURE |
| WOS记录号 | WOS:001048603900001 |
| 源URL | [http://119.78.100.183/handle/2S10ELR8/306881]  |
| 专题 | 中国科学院上海药物研究所 |
| 通讯作者 | Huang, He; Wei, Wei; Wong, Jiemin |
| 作者单位 | 1.East China Normal Univ, Wuhu Hosp, Wuhu, Anhui, Peoples R China 2.East China Normal Univ, Inst Biomed Sci, Shanghai Key Lab Regulatory Biol, Shanghai, Peoples R China 3.East China Normal Univ, Sch Life Sci, Shanghai, Peoples R China 4.Univ Chinese Acad Sci, Chinese Acad Sci, Shanghai Inst Nutr & Hlth, CAS Key Lab Computat Biol, Shanghai, Peoples R China 5.Chinese Acad Sci, Shanghai Inst Mat Med, Shanghai, Peoples R China 6.Fudan Univ, Inst Biomed Sci, Shanghai, Peoples R China |
| 推荐引用方式 GB/T 7714 | Li, Jialun,Lu, Lu,Liu, Lingling,et al. HDAC1/2/3 are major histone desuccinylases critical for promoter desuccinylation[J]. CELL DISCOVERY,2023,9(1):17. |
| APA | Li, Jialun.,Lu, Lu.,Liu, Lingling.,Ren, Xuelian.,Chen, Jiwei.,...&Wong, Jiemin.(2023).HDAC1/2/3 are major histone desuccinylases critical for promoter desuccinylation.CELL DISCOVERY,9(1),17. |
| MLA | Li, Jialun,et al."HDAC1/2/3 are major histone desuccinylases critical for promoter desuccinylation".CELL DISCOVERY 9.1(2023):17. |
入库方式： OAI收割
来源：上海药物研究所
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