{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nXRCC6, which encodes the Ku70 protein, plays a central role in the repair of DNA double‐strand breaks by classical nonhomologous end joining (NHEJ). Ku70 rapidly binds to exposed DNA termini and, as a heterodimer with Ku80, recruits and regulates the assembly of other repair factors such as DNA‐PKcs, XRCC4 and ligase IV. This binding not only facilitates end joining but also couples end‐processing (including 5′–deoxyribose phosphate lyase activity) and even modulates the extent of DNA end resection. In addition, structural analyses and studies of protein–protein interactions have mapped key domains in Ku70 that influence its association with accessory factors (for example, WRN to stimulate exonuclease activity), and have revealed mechanisms for its regulated removal from DNA ends—via p97 ATPase and PAXX—to ensure proper repair pathway choice."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "14"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its canonical role in DNA repair, XRCC6 is involved in maintaining genomic stability through telomere homeostasis and modulation of transcription. Ku70 associates with telomerase and directly binds telomerase RNA and the catalytic subunit (hTERT), thereby influencing telomere maintenance. In addition, genetic studies have implicated polymorphic variants of XRCC6 in cancer predisposition—including breast, oral, head and neck, and lung cancers—while interactions with transcriptional regulators such as BRG1 couple its DNA binding activity to hormone‐dependent gene expression. These findings indicate that Ku70 not only contributes to the repair of DNA damage but also integrates repair, telomere stabilization and transcriptional responses in a manner that impacts cell proliferation and aging."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "15", "end_ref": "29"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nXRCC6 also contributes to the regulation of apoptosis and innate immune responses. Deacetylation of Ku70 by SIRT1 modulates its capacity to interact with pro‐apoptotic factors such as Bax and p53, thereby influencing cell survival following stress. In some contexts, acetylation of Ku70 can lead to the release of Bax, promoting apoptosis, while Ku70 additionally functions as a deubiquitinase that stabilizes antiapoptotic proteins like Mcl-1. Remarkably, Ku70 is able to translocate from the nucleus to the cytoplasm—where, in complex with STING, it acts as a novel DNA sensor to induce type III interferon production—and it even serves as a receptor at the cell surface to mediate bacterial internalization. Collectively, these multifaceted roles highlight XRCC6 as a key integrator of DNA repair, apoptosis regulation and innate immunity."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "30", "end_ref": "39"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Pierre-Olivier Mari, Bogdan I Florea, Stephan P Persengiev, et al. 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