DHX9 phosphorylation at S321 by ATM regulates DHX9 retention at DNA double-strand break sites and interaction with BRCA1.

ABSTRACT: To preserve genome stability, the repair of DNA double-strand breaks (DSBs) that can be caused by exposure to ionizing radiation and certain anticancer drugs is of paramount importance. Recently, it became evident that various DNA-RNA helicases play a pivotal role in homologous recombination (HR) repair and non-homologous end joining, which are the two principal DSB repair machineries in mammalian cells. In a previous study, we reported that DHX9, which belongs to the DExH-box helicase family, is involved in HR repair. However, the regulatory mechanisms governing the function of DHX9 remains elusive. The present study has demonstrated that upon etoposide treatment, DHX9 was phosphorylated at S321 in a manner dependent on ataxia telangiectasia mutated (ATM), a protein kinase. In addition, c

SUBMITTER: Matsuya S 

PROVIDER: S-EPMC12446777 | biostudies-literature | 2025 Jul

REPOSITORIES: biostudies-literature