{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nU2AF2 (also known as the U2AF65 subunit) is a central, evolutionarily conserved splicing factor that mediates early steps in spliceosome assembly. By binding the polypyrimidine tract upstream of the 3′ splice site, U2AF2 plays a crucial role in defining intron–exon boundaries and recruiting other spliceosomal components such as U2 snRNP and U2AF35. Structural and biophysical studies reveal that its tandem RNA recognition motifs exhibit marked conformational plasticity—switching between closed and open states via induced fit and conformational selection—to accommodate degenerate pyrimidine signals. Such dynamic inter‐domain arrangements, together with critical side‐chain rearrangements and autoinhibitory contacts, enable U2AF2 to discriminate authentic splice signals from cryptic or suboptimal sequences, thereby ensuring both splicing fidelity and transcriptome integrity."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "26"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nU2AF2’s activity is further fine‐tuned by a host of trans‐acting regulators and posttranslational modifications. Specific enzymes, such as JMJD6, catalyze lysyl hydroxylation of U2AF2 to modulate its RNA binding and influence alternative splicing decisions. In addition, interactions with other splicing regulators—including factors like HNRNPA1 that can sequester or redirect U2AF2 binding, as well as associations with components of the transcription machinery—adjust its recruitment to bona fide versus decoy splice sites. Moreover, intrinsically disordered linker regions within U2AF2 provide an autoinhibitory “proofreading” function that helps prevent nonproductive interactions, thereby optimizing splice site selection."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "27", "end_ref": "34"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its canonical splicing function, aberrant regulation or modification of U2AF2 has been implicated in various disease contexts. In several cancers—including non–small cell lung cancer, castration-resistant prostate cancer, and melanoma—upregulated or stabilized U2AF2 promotes oncogenic alternative splicing events and supports metabolic reprogramming through pathways such as AKT/mTOR signaling. Other studies have linked U2AF2 to the nuclear export of toxic repeat-containing RNAs and to the formation of phase-separated condensates that modulate splice site selection. In some instances, cleavage of U2AF2 during apoptosis alters its activity, contributing to the dysregulation of alternative splicing programs that are associated with disease progression."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "35", "end_ref": "41"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Esther Kellenberger, Gunter Stier, Michael Sattler "}, {"type": "b", "children": [{"type": "t", "text": "Induced folding of the U2AF35 RRM upon binding to U2AF65."}]}, {"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)03294-5"}], "href": "https://doi.org/10.1016/s0014-5793(02"}, {"type": "t", "text": "03294-5) PMID: "}, {"type": "a", "children": [{"type": "t", "text": "12297299"}], "href": "https://pubmed.ncbi.nlm.nih.gov/12297299"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Dennis H Dowhan, Eugene P Hong, Didier Auboeuf, et al. 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"}, {"type": "b", "children": [{"type": "t", "text": "FRET analyses of the U2AF complex localize the U2AF35/U2AF65 interaction in vivo and reveal a novel self-interaction of U2AF35."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "RNA (2005)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1261/rna.7277705"}], "href": "https://doi.org/10.1261/rna.7277705"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "16043505"}], "href": "https://pubmed.ncbi.nlm.nih.gov/16043505"}]}, {"type": "r", "ref": 4, "children": [{"type": "t", "text": "Karen R Thickman, Matthew C Swenson, Joseph M Kabogo, et al. 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