Structure and function of the apical PIKKs in double-strand break repair

被引：4

作者：

Xu, Jingfei ^{[1
]}

Bradley, Noah ^{[1
]}

He, Yuan ^{[1
]}

机构：

[1] Northwestern Univ, Dept Mol Biosci, Evanston, IL 60208 USA

来源：

CURRENT OPINION IN STRUCTURAL BIOLOGY | 2023年 / 82卷

关键词：

DEPENDENT PROTEIN-KINASE; DNA-DAMAGE RESPONSE; CATALYTIC SUBUNIT; HOMOLOGOUS RECOMBINATION; PHOSPHORYLATION SITES; ATM ACTIVATION; IONIZING-RADIATION; LIGASE-IV; CRYO-EM; AUTOPHOSPHORYLATION;

D O I：

10.1016/j.sbi.2023.102651

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Members of the phosphatidylinositol 3' kinase (PI3K)-related mutated (ATM), ataxia-telangiectasia mutated and Rad3related (ATR), mammalian target of rapamycin (mTOR), suppressor with morphological effect on genitalia 1 (SMG1), and transformation/transcription domain-associated protein 1 (TRRAP/Tra1), participate in a variety of physiological processes, such as cell-cycle control, metabolism, transcription, replication, and the DNA damage response. In eukaryotic cells, DNA-PKcs, ATM, and ATR-ATRIP are the main sensors and regulators of DNA double-strand break repair. The purpose of this review is to describe recent structures of DNAPKcs, ATM, and ATR, as well as their functions in activation and phosphorylation in different DNA repair pathways.

引用

页数：12

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