{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nTP53BP2, which encodes ASPP2, is a multifunctional tumor suppressor best known for its capacity to enhance the apoptotic function of p53. ASPP2 directly binds p53 and its family members, thereby promoting the transcription of pro‐apoptotic target genes. Several studies demonstrate that bacterial virulence factors such as Helicobacter pylori CagA can subvert this apoptotic pathway by binding ASPP2 and inhibiting p53 activation, while oncogenic RAS cooperates with ASPP2 to stimulate p53‐dependent apoptosis. Moreover, transcriptional regulation by E2F further integrates ASPP2 into cell cycle and apoptotic control networks. These findings support a central role for TP53BP2/ASPP2 in modulating p53 function and cell death pathways."}, {"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 canonical role in apoptotic signaling through p53, ASPP2 is a key regulator of epithelial cell polarity and plasticity. It functions as a molecular switch governing epithelial-to-mesenchymal transition (EMT) and its reverse process, mesenchymal-to-epithelial transition (MET). ASPP2 enhances the localization of polarity proteins (for example, PAR3) at cell–cell junctions and can be disrupted by oncogenic factors or targeting by microRNAs such as miR-205, thereby provoking loss of junctional integrity, increased motility, and invasiveness. These alterations in cell polarity underlie the tumor-suppressive impact of ASPP2 in multiple cancers."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "8", "end_ref": "13"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nTP53BP2/ASPP2 also exerts critical control over cellular stress responses such as autophagy and senescence. Among hepatoma and other tumor cells, overexpression of ASPP2 can induce autophagic apoptosis through modulation of key mediators like CHOP and DRAM, while its inhibition is associated with enhanced autophagic flux and chemoresistance. In addition, downregulation of ASPP2 has been linked to aberrant lipid metabolism, such as activation of the mevalonate pathway in hepatocellular carcinoma, further connecting its loss to tumor progression. These studies highlight a dual role for ASPP2 in regulating survival pathways and determining chemosensitivity."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "14", "end_ref": "20"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn addition to its functions in apoptosis and autophagy, ASPP2 participates in the regulation of mitogenic and stress signaling networks. Through its interactions with proteins such as APP-BP1 it modulates protein neddylation, while its ability to bind Ras-GTP at the plasma membrane facilitates the stimulation of the Raf/MEK/ERK cascade leading to Ras-induced senescence. ASPP2 can also serve as a PP1-targeting subunit to regulate kinetochore-microtubule attachments during mitosis. Furthermore, posttranslational modifications including phosphorylation by MAPK further refine its capacity to enhance p53 functions. These diverse interactions underscore the importance of TP53BP2/ASPP2 as a nodal regulator that integrates signals from growth, survival and cell cycle checkpoints."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "21", "end_ref": "28"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nFinally, multiple studies have underscored the clinical and translational relevance of ASPP2. Epigenetic silencing and aberrant methylation of the TP53BP2 locus have been observed in various cancers, contributing to diminished ASPP2 expression and impaired apoptotic responses in tumors with wild-type p53. Its interplay with other key factors involved in insulin signaling and NF-κB pathways further implicates ASPP2 in metabolic regulation and inflammatory processes. Such dysregulation has been associated with poor prognosis, metastasis, and resistance to conventional therapies, emphasizing the potential of ASPP2 as both a prognostic biomarker and a therapeutic target."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "29", "end_ref": "34"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Ludovico Buti, Eric Spooner, Annemarthe G Van der Veen, et al. 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