{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nTankyrase 2 (TNKS2) is a poly(ADP‑ribose) polymerase that recognizes and binds specific substrate motifs via its ankyrin repeat clusters, thereby catalyzing PARylation to regulate substrate turnover. Through its PARylation of negative regulators such as AXIN, TNKS2 plays a central role in modulating canonical Wnt/β‑catenin signaling. In addition, its oligomerization mediated by the sterile α‑motif (SAM) domain supports both its scaffolding and catalytic activities, which are critical for the proper assembly of destruction complexes and maintenance of telomere homeostasis."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "4"}]}, {"type": "t", "text": ""}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn several cancers, deregulation of TNKS2 contributes to tumorigenesis by enhancing Wnt/β‑catenin–dependent transcription. Upregulation of TNKS2 has been observed in cervical cancer and triple‑negative breast cancer, where it promotes cell proliferation, migration, and invasion. Moreover, genetic variations in TNKS2 are associated with altered cancer risk in diverse malignancies including breast, laryngeal, and non‑small cell lung cancers, underscoring its relevance as an oncogenic driver."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "5", "end_ref": "14"}]}, {"type": "t", "text": ""}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its role in signaling, TNKS2 contributes to the regulation of chromosome stability and mitotic progression. It is involved in telomere length control and telomere cohesion, and its interaction network extends to proteins implicated in centrosomal and spindle pole maturation. Furthermore, TNKS2 associates with DNA damage response factors such as MDC1 to coordinate homologous recombination repair, highlighting its multifaceted role in preserving genomic integrity."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "15", "end_ref": "23"}]}, {"type": "t", "text": ""}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nTNKS2 also operates in the context of infectious and inflammatory processes. It can associate with viral and immune signaling proteins—as when it interacts with EBNA1 to inhibit viral DNA replication—and it modulates innate immune responses by PARylating targets such as VISA, thereby promoting their ubiquitin‑dependent degradation. Additionally, changes in TNKS2 expression influence host defense mechanisms during influenza infection and can affect autophagic processes in macrophages during tuberculosis."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "24", "end_ref": "28"}]}, {"type": "t", "text": ""}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nFinally, TNKS2 is an attractive therapeutic target. Small‑molecule inhibitors—including dual PARP/TNKS inhibitors such as E7449 and structurally optimized flavone derivatives—have been developed to disrupt TNKS2 activity and its downstream signaling, most notably in Wnt‑dependent cancers. Structure‑guided drug design, based on detailed insights into its catalytic domain and substrate interaction surfaces, further highlights the potential of TNKS2 inhibition as a means to modulate its diverse cellular functions."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "29", "end_ref": "32"}]}, {"type": "t", "text": ""}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Marinella G Callow, Hoanh Tran, Lilian Phu, et al. 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