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DNA双链断裂(double-strand breaks,DSBs)修复对于保证基因组完整性以及维持细胞的平衡稳定性起着关键作用。p53结合蛋白1(p53-binding protein 1,53BP1)是针对产生的双链断裂损伤做出反应的重要调控因子。目前,研究人员对于53BP1被招募到受损的染色质上的过程,以及53BP1在DSBs修复过程中阻止同源重组(homologous recombination,HR)的同时推动非同源末端连接(non-homologous end-joining,NHEJ)的过程,已经有了新的认识。并且,近期的研究结果启发科学家们提出了一种新的模型,即53BP1的招募需要直接识别DSBs特异性的组蛋白密码,而53BP1发挥作用时的通路选择则与BRCA1蛋白的拮抗作用有关。结合近年来有关53BP1的研究进展,主要综述了53BP1的结构与功能特点,其作为调控因子在DSBs修复过程中发挥的作用,以及53BP1达到有效聚集的方式。
Repair of DNA double-strand breaks (DSBs) plays a key role in ensuring genomic integrity and maintaining cell homeostasis. p53-binding protein 1, 53BP1 is an important regulator of response to double-stranded rupture damage produced. At present, the researchers have shown that 53BP1 is recruited to damaged chromatin and that 53BP1 promotes non-homologous end-joining (homologous recombination, HR) in the process of DSBs repair , NHEJ) process, there has been a new understanding. Moreover, recent findings have inspired scientists to propose a new model in which recruitment of 53BP1 requires a direct recognition of DSBs-specific histone codes, whereas pathway selection when 53BP1 is involved is associated with BRCA1 antagonism. Based on the recent progress in the research of 53BP1, we mainly reviewed the structure and function of 53BP1, the role of 53BP1 in the repair of DSBs as a regulator, and the way to achieve effective aggregation of 53BP1.