Quantitative Proteomics Reveals the Role of Lysine 2-Hydroxyisobutyrylation Pathway Mediated by Tip60
文献类型:期刊论文
作者 | Wang, Ning2; Jiang, Yue3,4; Peng, Ping5; Liu, Guobin1; Qi, Shankang4; Liu, Kun3; Mei, Qi5; Li, Jian6 |
刊名 | OXIDATIVE MEDICINE AND CELLULAR LONGEVITY
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出版日期 | 2022-02-08 |
卷号 | 2022页码:13 |
ISSN号 | 1942-0900 |
DOI | 10.1155/2022/4571319 |
通讯作者 | Qi, Shankang(qishankang@aliyun.com) ; Liu, Kun(kliu@mail.neu.edu.cn) ; Mei, Qi(qimei@tjh.tjmu.edu.cn) |
英文摘要 | Lysine 2-hydroxyisobutyrylation (Khib) is a new type of posttranslational modifications (PTMs) extensively reported on eukaryotic cell histones. It is evolutionarily conserved and participates in diverse important biological processes, such as transcription and cell metabolism. Recently, it has been demonstrated that Khib can be regulated by p300 and Tip60. Although the specific Khib substrates mediated by p300 have been revealed, how Tip60 regulates diverse cellular processes through the Khib pathway and the different roles between Tip60 and p300 in regulating Khib remain largely unknown, which prevents us from understanding how this modification executes its biological functions. In this study, we report the first Khib proteome mediated by Tip60. In total, 3502 unique Khib sites from 1050 proteins were identified. Among them, 536 Khib sites from 406 proteins were present only in Tip60 overexpressing cells and 13 Khib sites increased more than 2-fold in response to Tip60 overexpression, indicating that Tip60 significantly affected global Khib. Notably, only 5 of the 549 Tip60-targeted Khib sites overlapped with the 149 known Khib sites targeted by p300, indicating the different Khib substrate preferences of Tip60 and p300. In addition, the Khib substrates regulated by Tip60 are deeply involved in processes such as nucleic acid metabolism and translation, and some are associated with Parkinson's and Prion diseases. In summary, our research reveals the Khib substrates targeted by Tip60, which elucidates the effect of Tip60 in regulating various cellular processes through the Khib pathway, and proposes novel views into the functional mechanism of Tip60. |
WOS关键词 | HISTONE ; SYNTHASE ; HSP90 ; HDACS ; HATS |
资助项目 | Fundamental Research Funds for the Central Universities of the Ministry of Education[N2003010] ; Fundamental Research Funds for the Central Universities of the Ministry of Education[N2103027] |
WOS研究方向 | Cell Biology |
语种 | 英语 |
WOS记录号 | WOS:000766929000003 |
出版者 | HINDAWI LTD |
源URL | [http://119.78.100.183/handle/2S10ELR8/300206] ![]() |
专题 | 中国科学院上海药物研究所 |
通讯作者 | Qi, Shankang; Liu, Kun; Mei, Qi |
作者单位 | 1.Nanjing Univ Chinese Med, Sch Chinese Mat Med, Nanjing 210023, Peoples R China 2.Xi An Jiao Tong Univ, Dept Neurosurg, Affiliated Hosp 1, Xian 710061, Peoples R China 3.Northeastern Univ, Sch Mech Engn & Automat, Shenyang 110819, Peoples R China 4.Chinese Acad Sci, Shanghai Inst Mat Medica, Shanghai 201203, Peoples R China 5.Huazhong Univ Sci & Technol, Tongji Hosp, Dept Oncol, Tongji Med Coll, Wuhan 430030, Peoples R China 6.Univ Clin Rhein Friedrich Wilhelms Univ, Inst Mol Med & Expt Immunol, Bonn, Germany |
推荐引用方式 GB/T 7714 | Wang, Ning,Jiang, Yue,Peng, Ping,et al. Quantitative Proteomics Reveals the Role of Lysine 2-Hydroxyisobutyrylation Pathway Mediated by Tip60[J]. OXIDATIVE MEDICINE AND CELLULAR LONGEVITY,2022,2022:13. |
APA | Wang, Ning.,Jiang, Yue.,Peng, Ping.,Liu, Guobin.,Qi, Shankang.,...&Li, Jian.(2022).Quantitative Proteomics Reveals the Role of Lysine 2-Hydroxyisobutyrylation Pathway Mediated by Tip60.OXIDATIVE MEDICINE AND CELLULAR LONGEVITY,2022,13. |
MLA | Wang, Ning,et al."Quantitative Proteomics Reveals the Role of Lysine 2-Hydroxyisobutyrylation Pathway Mediated by Tip60".OXIDATIVE MEDICINE AND CELLULAR LONGEVITY 2022(2022):13. |
入库方式: OAI收割
来源:上海药物研究所
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