{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nNONO, also known as p54(nrb), is a multifunctional nuclear protein belonging to the DBHS family that operates as an integral component of diverse nuclear processes. Early studies identified NONO in the context of transcriptional regulation and splicing, and subsequent work has shown that it forms obligate heterodimers with partners such as PSF, participates in coupling RNA‐polymerase II elongation with spliceosome assembly, and contributes to the formation of paraspeckles – specialized nuclear bodies that sequester specific RNAs. In addition, NONO has been implicated in regulating pre‐mRNA processing through its interaction with spliceosomal U5 small nuclear RNA elements and various RNA‐binding proteins."}, {"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": "\nNONO also functions prominently in RNA processing and post‐transcriptional regulation. It modulates the biogenesis of microRNAs by interacting, as part of a NONO–PSF heterodimer complex, with the primary transcripts to facilitate Drosha–DGCR8 Microprocessor processing. Moreover, it contributes to transcription termination through recruitment of 3′ processing factors such as XRN2, and it regulates alternative splicing – partly through interactions with other splicing regulators like hnRNP M – thus influencing both splice-site selection and mRNA maturation. These roles are further tuned by post‐translational modifications (for example, phosphorylation by MAP kinase–interacting kinases) that can alter NONO’s RNA binding affinity and its association with messenger ribonucleoprotein complexes."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "12", "end_ref": "18"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn the context of genomic integrity, NONO plays a critical role in the DNA damage response. It is rapidly recruited to sites of double-strand breaks, where the NONO–PSF complex has been shown to facilitate end joining by promoting sequence-independent DNA pairing and by functionally substituting for classical NHEJ factors such as XLF. Moreover, NONO is targeted for ubiquitination by factors such as RNF8 following UV-induced DNA damage, and its regulated degradation appears necessary for the proper resolution of checkpoint signalling."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "19", "end_ref": "22"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nDysregulation of NONO has emerged as a significant factor in several human pathologies, notably various cancers and developmental disorders. Elevated NONO expression or aberrant post‐translational modification (e.g. methylation by PRMT1) has been linked to oncogenic processes by enhancing the stability of transcription factors like SREBP‐1a to promote lipogenesis in breast cancer, by interacting with long noncoding RNAs to drive metastasis in colorectal cancer, and by modulating the activity of nuclear receptors that influence tumor progression in hormone‐dependent and triple‐negative breast cancers. Moreover, genomic rearrangements that fuse NONO with TFE3 have defined distinct renal cell carcinoma subtypes, while loss‐of‐function mutations in NONO are associated with intellectual disability, cardiomyopathy, and synaptic defects. Additional studies implicate NONO in altering nucleolar stress responses and c-Myc translation, further underscoring its multifaceted roles in tumorigenesis and developmental regulation."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "23", "end_ref": "35"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nNONO also influences viral infections by interacting directly with viral RNAs and host factors involved in viral mRNA metabolism. Studies have demonstrated that NONO binds to specific cis-acting elements in transcripts of viruses such as hepatitis delta virus, thereby engaging components of the host RNA processing machinery, and that it negatively regulates HIV-1 infection through mechanisms that modulate the efficiency of viral reverse transcription and gene expression."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "36"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "M Pavao, Y H Huang, L J Hafer, et al. 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