{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nRYBP (Ring1‐ and YY1‐binding protein) was first identified as a key mediator of transcription factor specificity by bridging E2F2/E2F3 with YY1 to activate critical cell cycle genes such as Cdc6."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "1"}]}, {"type": "t", "text": " Subsequent studies using tumor‐selective models demonstrated that exogenous expression of RYBP, also known as DEDAF, potently induces apoptosis in transformed cells."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "2"}]}, {"type": "t", "text": " Furthermore, adenovirus‐mediated delivery of RYBP has been shown to inhibit proliferation and trigger apoptotic cell death preferentially in tumor cells, underscoring its anticancer potential."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "4"}]}, {"type": "t", "text": " In addition, through a direct interaction with MDM2, RYBP markedly reduces p53 ubiquitination, thereby stabilizing and activating p53‐dependent tumor suppressor pathways."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "5"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn diverse cancer models – including hepatocellular carcinoma (HCC), esophageal squamous cell carcinoma, anaplastic thyroid cancer, and head and neck squamous cell carcinoma – RYBP expression is frequently diminished, correlating with enhanced tumor cell proliferation, invasion, and chemoresistance. Overexpression of RYBP in these contexts not only inhibits cell growth and metastatic behavior but also improves chemosensitivity."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "6"}]}, {"type": "t", "text": " Transcriptional regulation by factors such as KLF4 and Sp1 further modulates RYBP levels in HCC, and genetic as well as microRNA-mediated regulation – for example, by miR-769-5p and SNP variants – has been implicated in disease progression and patient prognosis."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "8", "end_ref": "10"}]}, {"type": "t", "text": " Moreover, the proper subcellular localization of RYBP, dictated by intrinsic nuclear localization signals (NLSs), is critical for its ability to interact with caspase 8 and enforce p53 stabilization, influencing its tumor-suppressive activity."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "11"}]}, {"type": "t", "text": " Its tumor suppressor function has also been confirmed in esophageal"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "12"}]}, {"type": "t", "text": "and anaplastic thyroid cancers"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "13"}]}, {"type": "t", "text": ", and ETS1-driven upregulation of RYBP has been shown to contribute to growth inhibition partly via p21 induction."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "14"}]}, {"type": "t", "text": " In head and neck squamous cell carcinoma, miR-411-5p–mediated downregulation of RYBP accentuates metastatic behaviors, further substantiating its role in suppressing tumor progression."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "15"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nRYBP also functions as a central component of noncanonical Polycomb repressive complex 1 (PRC1), where it enhances chromatin compaction and gene silencing. A recent review has underscored its developmental and mechanistic roles in epigenetic regulation and apoptosis."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "16"}]}, {"type": "t", "text": " Detailed biochemical studies have defined an NLS region within RYBP that mediates binding to importin proteins, thereby controlling its nuclear import."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "17"}]}, {"type": "t", "text": " Loss of RYBP function has been linked to aberrant CpG island hypermethylation and transformation, emphasizing its role in maintaining proper epigenetic landscapes."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "18"}]}, {"type": "t", "text": " In parallel, overexpression of RYBP attenuates ATM kinase activation and recruitment to DNA damage sites, which sensitizes tumor cells to poly-ADP-ribose polymerase inhibitors."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "19"}]}, {"type": "t", "text": " Mechanistically, RYBP stabilizes Ring1B by antagonizing its ubiquitination via UBE3A and, together with its inherent capacity to bind ubiquitin on H2Aub1-modified nucleosomes, reinforces transcriptional repression."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "20"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nAdditional emerging roles highlight the multifaceted regulation of RYBP. Low RYBP levels in HCC have been reported as a robust prognostic marker, outperforming conventional markers such as AFP."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "22"}]}, {"type": "t", "text": " In metabolic regulation, high glucose conditions in tumor cells suppress RYBP degradation, which in turn negatively regulates glycolytic flux and cell migration."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "23"}]}, {"type": "t", "text": " Moreover, in preeclampsia, a circRNA-mediated sponging of miR-558 leads to upregulation of RYBP, promoting trophoblast dysfunction, while interaction with plakophilin 1 (PKP1) may serve to counteract epithelial-to-mesenchymal transition and metastasis in cancer cells."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "24"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Susanne Schlisio, Terri Halperin, Miguel Vidal, et al. 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