{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nCtIP (RBBP8) is emerging as a central regulator of DNA double‐strand break (DSB) repair through homologous recombination. In S and G2 phases, CtIP is recruited in a highly regulated, phosphorylation‐dependent manner to initiate 5′-to-3′ DNA end resection—generating 3′ single‐stranded DNA overhangs essential for RAD51 filament formation and strand invasion. Through direct physical and functional interactions with the Mre11/Rad50/Nbs1 (MRN) complex and BRCA1, CtIP couples DSB sensing with processing, thereby ensuring efficient activation of ATR‐dependent checkpoint signalling and precise DSB repair. Its activity is tightly controlled by cell cycle kinases (e.g., CDK) that phosphorylate key residues such as Ser327 and Thr847, thereby modulating its nuclease‐independent functions and its interplay with other repair proteins."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "18"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its canonical role in promoting homologous recombination, CtIP also exerts critical functions in governing repair pathway choice and the processing of complex DSB ends. By modulating the balance between canonical non-homologous end joining, alternative end joining, and homologous recombination, CtIP—often in cooperation with factors such as 53BP1, RNF138, USP4, and PLK3—regulates the extent of DNA resection. Its post-translational modifications (including ubiquitylation and sumoylation) and dynamic interaction with additional repair proteins further coordinate critical transitions such as the removal of Ku from DNA ends and the recovery of stalled replication forks. These multifaceted regulatory events ensure that CtIP not only activates resection at damage sites but also tailors the repair process to the nature of the lesion and the cell cycle context."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "19", "end_ref": "35"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nAlterations in CtIP expression, mutations truncating its C-terminal sequences, or disruptions in its regulatory interactions have important pathological and clinical implications. Deficiencies in CtIP or aberrant post-translational regulation are associated with genomic instability, altered responses to DNA-damaging agents, and inherited conditions such as Seckel and Jawad syndromes. Moreover, changes in CtIP levels have been linked to tumor progression and therapy resistance—in particular, impacting breast and myeloid cancers through defective homologous recombination repair and perturbations in transcriptional networks. Collectively, these findings underscore the multifaceted role of CtIP in maintaining genome integrity and highlight its potential as a biomarker and therapeutic target in oncogenesis."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "36", "end_ref": "42"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Eleanor Y M Sum, Benjamin Peng, Xin Yu, et al. 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