{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nThe NBN‐encoded protein (commonly referred to as NBS1) is a pivotal component of the MRE11–RAD50–NBS1 (MRN) complex that functions as an early sensor of DNA double‐strand breaks. It plays an essential role in recruiting and activating the ataxia–telangiectasia mutated (ATM) kinase and other damage‐responsive effectors, thereby triggering checkpoint signalling and coordinated chromatin changes at break sites. Key to this function are its conserved forkhead‐associated (FHA) and BRCA1 C‐terminal (BRCT) domains that interact in a phosphorylation‐dependent manner with adaptor proteins such as MDC1 and are required for stable retention of complex members at DNA lesions."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "7"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its role in initial damage recognition, NBS1 orchestrates subsequent DNA repair processes. It facilitates DNA end resection and the homologous recombination repair pathway – in part through its regulated interactions with proteins such as CtIP – and modulates the engagement and processivity of downstream nucleases and helicases. This multifaceted activity is further fine‐tuned by post‐translational modifications (for example, phosphorylation and acetylation) that adjust its binding affinity and interactions with other repair factors. In doing so, NBS1 not only couples repair to cell‐cycle regulation but also helps ensure proper DNA replication, telomere maintenance, and processing of complex DNA lesions."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "8", "end_ref": "22"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nDefects or mutations in NBS1 can compromise these critical functions, leading to genomic instability and contributing to cancer susceptibility. In various studies, impaired NBS1 function has been linked not only to defective DSB repair and checkpoint signalling but also to deregulated cellular responses such as premature senescence and altered cytokine secretion that in turn may influence the tumour microenvironment. Consistent with these observations, polymorphisms or reduced expression of NBS1 have been associated with an increased risk for malignancies including breast, lung, prostate, and bladder cancers, thereby underscoring the multifaceted impact of NBS1 on genome integrity and cellular homeostasis."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "23", "end_ref": "30"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Travis H Stracker, Christian T Carson, Matthew D Weitzman "}, {"type": "b", "children": [{"type": "t", "text": "Adenovirus oncoproteins inactivate the Mre11-Rad50-NBS1 DNA repair complex."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Nature (2002)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/nature00863"}], "href": "https://doi.org/10.1038/nature00863"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "12124628"}], "href": "https://pubmed.ncbi.nlm.nih.gov/12124628"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Magtouf Gatei, Katie Sloper, Claus Sorensen, et al. 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