{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nSFPQ (also known as PSF) is a conserved, multifunctional nuclear protein that plays pivotal roles in RNA biogenesis and transcriptional regulation. It participates in pre‐mRNA splicing and alternative splicing events, and its ability to form dynamic higher‐order assemblies underlies the organization of nuclear bodies such as paraspeckles. In concert with its binding partner NONO, SFPQ couples transcription with RNA processing—for example, by linking strong transcriptional activators and the RNA polymerase II C‐terminal domain to specific splicing decisions, modulating pathways such as IRES‐dependent translation of key regulators (including p53) and the splicing of immune transcripts (e.g. CD45). Moreover, SFPQ is targeted by long noncoding RNAs (such as NEAT1 and MALAT1) that, by redistributing SFPQ within the nucleus, contribute to stimulus‐responsive gene expression (e.g. activation of antiviral cytokines) and impact tumor progression. Its structural features—including extended coiled‐coil domains that allow polymerization—are essential for these regulatory functions."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "13"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn addition to its central roles in RNA processing, SFPQ is crucial for maintaining genomic stability. It participates in the repair of DNA double‐strand breaks by promoting nonhomologous end joining and homologous recombination—interacting directly with repair factors such as RAD51 and facilitating 3′ end processing via the recruitment of exonucleases like XRN2. Post‐translational modifications, including phosphorylation by oncogenic kinases (e.g. NPM/ALK), further modulate SFPQ’s repair activities. Disruption of these regulatory processes—manifest as aberrant splicing of its own transcript, altered nuclear retention, or sensitivity to replication stress (notably in BRAFV600E–driven tumors)—has been linked to neurodegenerative conditions such as tauopathies and ALS."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "14", "end_ref": "24"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nSFPQ also influences diverse cellular outcomes by modulating host–pathogen interactions, oncogenic signaling, and neuronal function. On one hand, it binds viral RNA elements—regulating the stability, transport, and translation of transcripts from pathogens such as HIV, Coxsackievirus, and influenza virus—and is even detectable at the cell surface where it can mediate bacterial invasion in meningitis. On the other hand, aberrant SFPQ activity contributes to tumorigenesis through gene fusions (as seen in SFPQ–TFE3 renal carcinomas) and by partnering with specific long noncoding RNAs (such as GAPLINC) to promote cellular invasion and chemoresistance. In neurons, SFPQ associates with kinesin motor complexes to facilitate long‐distance RNA transport, while its misregulation also underlies defects in circRNA biogenesis that may compromise neuronal homeostasis. Collectively, these roles position SFPQ as a central regulator whose multifaceted activities impact RNA metabolism, DNA repair, and cellular signaling in both health and disease."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "25", "end_ref": "34"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Yaron Shav-Tal, Dov Zipori "}, {"type": "b", "children": [{"type": "t", "text": "PSF and p54(nrb)/NonO--multi-functional nuclear proteins."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "FEBS Lett (2002)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/s0014-5793(02)03447-6"}], "href": "https://doi.org/10.1016/s0014-5793(02"}, {"type": "t", "text": "03447-6) PMID: "}, {"type": "a", "children": [{"type": "t", "text": "12417296"}], "href": "https://pubmed.ncbi.nlm.nih.gov/12417296"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Emanuel Rosonina, Joanna Y Y Ip, John A Calarco, et al. 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