{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nU2AF1 encodes a key auxiliary splicing factor that is essential for accurate pre‐mRNA intron removal by specifically recognizing the invariant AG dinucleotide at the 3′ splice site. Structural and biochemical studies have demonstrated that U2AF1, together with its partner U2AF65, helps define functional 3′ splice sites through its conserved zinc finger domains and RNA recognition motifs. These investigations established that U2AF1’s normal function is to “read” specific nucleotide signals located immediately upstream of exons, thereby guiding spliceosome assembly and ensuring proper exon–intron definition."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "6"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nRecurrent somatic mutations in U2AF1—most notably missense changes such as S34F and Q157 alterations—cause allele‐specific shifts in RNA binding and 3′ splice site preference. These mutations lead to widespread, although quantitatively subtle, changes in alternative splicing patterns, characterized by enhanced exon skipping, intron retention, and the differential selection of splice sites. Such aberrant splicing affects diverse pathways including DNA methylation, damage response, cell cycle regulation, apoptosis, and even immune signalling (via effects on cytokine and innate immune factor isoforms, as exemplified by the preferential production of an “active” IRAK4 isoform). In hematologic malignancies like myelodysplastic syndromes, acute myeloid leukemia and chronic myelomonocytic leukemia, U2AF1 mutations are frequently encountered and are often associated with distinct clinical phenotypes and prognostic implications."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "7", "end_ref": "22"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its canonical role in splice site recognition, mutant U2AF1 exerts broader effects that include alteration of mRNA translation and modulation of stress or inflammatory responses. For example, interactions between bacterial effectors and U2AF1 have been implicated in the regulation of host cytokine gene expression, while the mutant protein—in addition to its splicing misregulation—has been shown to impair proper cell differentiation and even disrupt cell cycle progression by altering isoform expression of key regulators. Intriguingly, analyses of alternative U2AF1 transcript isoforms further suggest that the balance among its variants may itself be critical for cell division and normal RNA processing. These additional noncanonical functions and the sensitivity of mutant cells to pharmacological spliceosome modulators underscore U2AF1’s potential as both a biomarker and a therapeutic target in disorders ranging from hematologic malignancies to aberrant inflammatory states."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "23", "end_ref": "28"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Wei-Qun Ding, Susan M Kuntz, Laurence J Miller "}, {"type": "b", "children": [{"type": "t", "text": "A misspliced form of the cholecystokinin-B/gastrin receptor in pancreatic carcinoma: role of reduced sellular U2AF35 and a suboptimal 3'-splicing site leading to retention of the fourth intron."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Cancer Res (2002)"}]}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "11830556"}], "href": "https://pubmed.ncbi.nlm.nih.gov/11830556"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Teresa R Pacheco, Miguel B Coelho, Joana M P Desterro, et al. 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