Multifaceted regulation and functions of 53BP1 in NHEJ-mediated DSB repair (Review)

作者全名："Lei, Tiantian; Du, Suya; Peng, Zhe; Chen, Lin"

作者地址："[Lei, Tiantian; Peng, Zhe; Chen, Lin] Chongqing Med Univ, Dept Pharm, Women & Childrens Hosp, Chongqing 401147, Peoples R China; [Du, Suya] Univ Elect Sci & Technol China, Sichuan Canc Hosp & Inst, Dept Clin Pharm, Sichuan Canc Ctr,Sch Med, Chengdu 610041, Sichuan, Peoples R China; [Chen, Lin] Chongqing Med Univ, Dept Pharm, Women & Childrens Hosp, 120 Longshan Rd, Chongqing 401147, Peoples R China"

通信作者："Chen, L (通讯作者)，Chongqing Med Univ, Dept Pharm, Women & Childrens Hosp, 120 Longshan Rd, Chongqing 401147, Peoples R China."

来源：INTERNATIONAL JOURNAL OF MOLECULAR MEDICINE

ESI学科分类：CLINICAL MEDICINE

WOS号：WOS:000806800600001

JCR分区：Q1

影响因子：5.4

年份：2022

卷号：50

期号：1

开始页：　

结束页：　

文献类型：Review

关键词：p53-binding protein 1; DNA double strand break; non-homologous end joining; RAP1-interacting factor 1; Pax transactivation domain-interacting protein

摘要："The repair of DNA double-strand breaks (DSBs) is crucial for the preservation of genomic integrity and the maintenance of cellular homeostasis. Non-homologous DNA end joining (NHEJ) is the predominant repair mechanism for any type of DNA DSB during the majority of the cell cycle. NHEJ defects regulate tumor sensitivity to ionizing radiation and anti-neoplastic agents, resulting in immunodeficiencies and developmental abnormalities in malignant cells. p53-binding protein 1 (53BP1) is a key mediator involved in DSB repair, which functions to maintain a balance in the repair pathway choices and in preserving genomic stability. 53BP1 promotes DSB repair via NHEJ and antagonizes DNA end overhang resection. At present, novel lines of evidence have revealed the molecular mechanisms underlying the recruitment of 53BP1 and DNA break-responsive effectors to DSB sites, and the promotion of NHEJ-mediated DSB repair via 53BP1, while preventing homologous recombination. In the present review article, recent advances made in the elucidation of the structural and functional characteristics of 53BP1, the mechanisms of 53BP1 recruitment and interaction with the reshaping of the chromatin architecture around DSB sites, the post-transcriptional modifications of 53BP1, and the up- and downstream pathways of 53BP1 are discussed. The present review article also focuses on the application perspectives, current challenges and future directions of 53BP1 research."

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