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AMPK-mediated phosphorylation on 53BP1 promotes c-NHEJ

文献类型：期刊论文

作者Jiang, Yuejing2,3; Dong, Ying2,3; Luo, Yifeng3,4; Jiang, Shangwen5; Meng, Fei-Long3,4; Tan, Minjia3,5; Li, Jia1,2,3,6; Zang, Yi2,3,6
刊名CELL REPORTS
出版日期2021-02-16
卷号34期号:7页码:22
ISSN号2211-1247
DOI10.1016/j.celrep.2021.108713
通讯作者Li, Jia(jli@simm.ac.cn) ; Zang, Yi(yzang@simm.ac.cn)
英文摘要AMP-activated protein kinase (AMPK) is an energy sensor that plays roles in multiple biological processes beyond metabolism. Several studies have suggested that AMPK is involved in the DNA damage response (DDR), but the mechanisms remain unclear. Herein, we demonstrate that AMPK promotes classic non-homologous end joining (c-NHEJ) in double-strand break (DSB) repair through recruiting a key chromatin-based mediator named p53-binding protein 1 (53BP1), which facilitates the end joining of distal DNA ends during DDR. We find that the interaction of AMPK and 53BP1 spatially occurs under DSB stress. In the context of DSBs, AMPK directly phosphorylates 53BP1 at Ser1317 and promotes 53BP1 recruitment during DDR for an efficient c-NHEJ, thus maintaining genomic stability and diversity of the immune repertoire, Taken together, our study demonstrates that AMPK is a regulator of 53BP1 and controls c-NHEJ choice by phospho-regulation.
WOS关键词ACTIVATED PROTEIN-KINASE ; CLASS SWITCH RECOMBINATION ; STRAND BREAK REPAIR ; DAMAGE RESPONSE ; CELL-CYCLE ; DNA ; ATM ; PATHWAY ; MECHANISM ; RADIOSENSITIZATION
资助项目National Natural Science Foundation of China[31871414] ; National Natural Science Foundation of China[81673489] ; National Natural Science Foundation of China[81821005] ; National Science Fund for Distinguished Young Scholars[81125023] ; Shanghai Science and Technology Development Funds[19JC1416300] ; Shanghai Science and Technology Development Funds[19YF1457500] ; K. C. Wong Education Foundation
WOS研究方向Cell Biology
语种英语
WOS记录号WOS:000619786600001
出版者CELL PRESS
源URL[http://119.78.100.183/handle/2S10ELR8/295652]  
专题新药研究国家重点实验室
通讯作者Li, Jia; Zang, Yi
作者单位1.Pilot Natl Lab Marine Sci & Technol Qingdao, Open Studio Druggabil Res Marine Nat Prod, 1 Wenhai Rd, Qingdao 266237, Peoples R China
2.Chinese Acad Sci, Shanghai Inst Mat Med, State Key Lab Drug Res, Shanghai 201203, Peoples R China
3.Univ Chinese Acad Sci, 19A Yuquan Rd, Beijing 100049, Peoples R China
4.Chinese Acad Sci, CAS Ctr Excellence Mol Cell Sci, Shanghai Inst Biochem & Cell Biol, State Key Lab Mol Biol, 320 Yueyang Rd, Shanghai 200031, Peoples R China
5.Chinese Acad Sci, Chem Prote Ctr, Shanghai Inst Mat Med, State Key Lab Drug Res, Shanghai 201203, Peoples R China
6.UCAS, Hangzhou Inst Adv Study, Sch Pharmaceut Sci & Technol, Hangzhou 310024, Peoples R China
推荐引用方式
GB/T 7714		 Jiang, Yuejing,Dong, Ying,Luo, Yifeng,et al. AMPK-mediated phosphorylation on 53BP1 promotes c-NHEJ[J]. CELL REPORTS,2021,34(7):22.
APA Jiang, Yuejing.,Dong, Ying.,Luo, Yifeng.,Jiang, Shangwen.,Meng, Fei-Long.,...&Zang, Yi.(2021).AMPK-mediated phosphorylation on 53BP1 promotes c-NHEJ.CELL REPORTS,34(7),22.
MLA Jiang, Yuejing,et al."AMPK-mediated phosphorylation on 53BP1 promotes c-NHEJ".CELL REPORTS 34.7(2021):22.

入库方式： OAI收割

来源：上海药物研究所

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