{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nTankyrase (TNKS) enzymes are multifunctional poly(ADP‐ribose) polymerases that play a central role in telomere homeostasis and mitosis. They regulate telomere length by binding to telomeric proteins such as TRF1 and, through their PARP activity, modify and displace these factors to allow telomerase access. In human cells, TNKS‐mediated PARsylation is critical not only for releasing TRF1 from telomeres to promote elongation but also for ensuring proper resolution of sister chromatid cohesion at telomeres during mitosis. In this context, TNKS orchestrates the removal of lingering protein complexes (for example, by PARsylating NuMA) to enable timely spindle pole formation and faithful chromosome segregation."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "11"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nTNKS also exerts a pivotal influence over key signaling pathways. By poly(ADP‐ribosyl)ating crucial scaffold proteins such as Axin, tankyrase destabilizes the β‐catenin destruction complex thereby enhancing Wnt/β‐catenin signaling—a mechanism that is implicated in several cancers. In addition, TNKS activity is linked to the modulation of Notch receptor trafficking and turnover, serving to fine‐tune cell fate–determining pathways. These signaling functions, together with roles in drug resistance and cancer cell proliferation, have made TNKS an attractive therapeutic target that is being exploited with small‐molecule inhibitors."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "12", "end_ref": "19"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond these roles, TNKS functions as a versatile molecular scaffold through its multiple ankyrin repeat clusters that mediate interactions with a wide array of proteins—including binding partners such as TAB182, Mcl-1 isoforms, and even viral factors like EBNA1. This capacity to engage diverse targets facilitates its regulation of protein turnover via subsequent ubiquitin-mediated degradation and situates TNKS as an integrator of processes ranging from DNA repair (by stabilizing factors like DNA-PKcs) to peroxisome homeostasis. Moreover, genetic variants in TNKS have been implicated in metabolic traits and cancer susceptibility, and small-molecule inhibitors that target its PARP activity (often in dual inhibition with other PARPs) have shown promise in preclinical cancer models. Collectively, these findings underscore TNKS as a central regulator of cellular homeostasis whose dysregulation contributes to a spectrum of human pathologies."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "20"}, {"type": "fg_f", "ref": "6"}, {"type": "fg_fs", "start_ref": "22", "end_ref": "30"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Hiroyuki Seimiya, Susan Smith "}, {"type": "b", "children": [{"type": "t", "text": "The telomeric poly(ADP-ribose) polymerase, tankyrase 1, contains multiple binding sites for telomeric repeat binding factor 1 (TRF1) and a novel acceptor, 182-kDa tankyrase-binding protein (TAB182)."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2002)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M112266200"}], "href": "https://doi.org/10.1074/jbc.M112266200"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "11854288"}], "href": "https://pubmed.ncbi.nlm.nih.gov/11854288"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Juan I Sbodio, Nai-Wen Chi "}, {"type": "b", "children": [{"type": "t", "text": "Identification of a tankyrase-binding motif shared by IRAP, TAB182, and human TRF1 but not mouse TRF1. 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