AMPK-mediated phosphorylation on 53BP1 promotes c-NHEJ

doi:10.1016/j.celrep.2021.108713

	AMPK-mediated phosphorylation on 53BP1 promotes c-NHEJ
	Jiang, Yuejing 3,4; Dong, Ying 3,4; Luo, Yifeng 4,5; Jiang, Shangwen 6; Meng, Fei-Long 4,5; Tan, Minjia 4,6; Li, Jia 1,2,3,4; Zang, Yi 2,3,4
刊名	CELL REPORTS
	2021-02-16
卷号	34 期号:7 页码:22
ISSN号	2211-1247
DOI	10.1016/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.
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关键词	ACTIVATED PROTEIN-KINASE ; CLASS SWITCH RECOMBINATION ; STRAND BREAK REPAIR ; DAMAGE RESPONSE ; CELL-CYCLE ; DNA ; ATM ; PATHWAY ; MECHANISM ; RADIOSENSITIZATION
WOS研究方向	Cell Biology
语种	英语
出版者	CELL PRESS
WOS记录号	WOS:000619786600001
内容类型	期刊论文
源URL	[http://119.78.100.183/handle/2S10ELR8/295652]
专题	中国科学院上海药物研究所
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.UCAS, Hangzhou Inst Adv Study, Sch Pharmaceut Sci & Technol, Hangzhou 310024, Peoples R China 3.Chinese Acad Sci, Shanghai Inst Mat Med, State Key Lab Drug Res, Shanghai 201203, Peoples R China 4.Univ Chinese Acad Sci, 19A Yuquan Rd, Beijing 100049, Peoples R China 5.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 6.Chinese Acad Sci, Chem Prote Ctr, Shanghai Inst Mat Med, State Key Lab Drug Res, Shanghai 201203, 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.