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• W2762298519 abstract "Abstract MDC1 plays a critical role in the DNA damage response (DDR) by interacting directly with several factors including γ-H2AX. However, the mechanism by which MDC1 is recruited to damaged sites remains elusive. Here, we show that MDC1 interacts with a helix–loop–helix (HLH)-containing protein called inhibitor of DNA-binding 3 (ID3). In response to double-strand breaks (DSBs) in the genome, ATM phosphorylates ID3 at serine 65 within the HLH motif, and this modification allows a direct interaction with MDC1. Moreover, depletion of ID3 results in impaired formation of ionizing radiation (IR)-induced MDC1 foci, suppression of γ-H2AX-bound MDC1, impaired DSB repair, cellular hypersensitivity to IR, and genomic instability. Disruption of the MDC1–ID3 interaction prevents accumulation of MDC1 at sites of DSBs and suppresses DSB repair. Thus, our study uncovers an ID3-dependent mechanism of recruitment of MDC1 to DNA damage sites and suggests that the ID3–MDC1 interaction is crucial for DDR." @default.
• W2762298519 created "2017-10-20" @default.
• W2762298519 creator A5000295358 @default.
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• W2762298519 date "2017-10-12" @default.
• W2762298519 modified "2023-09-24" @default.
• W2762298519 title "ID3 regulates the MDC1-mediated DNA damage response in order to maintain genome stability" @default.
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• W2762298519 doi "https://doi.org/10.1038/s41467-017-01051-z" @default.
• W2762298519 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/5638908" @default.
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• W2762298519 hasPublicationYear "2017" @default.
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