{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nRUVBL2 is a highly conserved AAA+ ATPase that, together with its partner RUVBL1, forms dynamic multimeric assemblies essential for the biogenesis and regulation of numerous macromolecular complexes. It plays a central role in chromatin remodeling (through complexes such as INO80, SWR1, TIP60 and the R2TP/PAQosome), telomerase assembly, snoRNP maturation, and transcription regulatory processes. Structural studies have revealed that RUVBL2–RUVBL1 complexes adopt hexameric or dodecameric ring‐shaped conformations and that their ATPase activity is modulated by nucleotide binding, conformational changes in an inserted domain II, and post‐translational modifications. These molecular insights also underscore how RUVBL2 acts as a chaperone by mediating the assembly and stability of large protein machines, thereby coordinating essential nuclear activities."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "17"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn the context of cancer and DNA repair, RUVBL2 supports oncogenic programs by facilitating the assembly and activity of telomerase, modulating transcription factors (such as c‐MYB and β‑catenin), and coordinating DNA damage responses. Its overexpression in various tumors—including hepatocellular, renal, and hematologic malignancies—contributes to cell proliferation, survival, metastatic potential, and aberrant signal transduction (for example, via altered PI3K/AKT and insulin signalling pathways). RUVBL2 thereby serves as an essential cofactor that not only assists in the formation of critical regulatory complexes but also governs the stability of key oncogenic proteins, making it a potential therapeutic target in multiple cancer types."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "18", "end_ref": "27"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its roles in nuclear processes, RUVBL2 is also implicated in host–pathogen interactions and additional quality control mechanisms. It influences viral replication by modulating the assembly of viral ribonucleoprotein complexes—influenza virus nucleoprotein oligomerization is suppressed by RUVBL2, while HIV-1 exploits RUVBL2 to fine-tune the balance of structural and envelope proteins, and Ebola virus nucleoprotein recruits RUVBL2-containing complexes during capsid formation. 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