{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nNXF1, also known as TAP, is a highly conserved, modular mRNA export receptor that plays a central role in the nucleocytoplasmic transport of fully processed messenger ribonucleoprotein (mRNP) complexes. Its distinct domains—the RNA recognition motif (RRM), leucine‐rich repeat (LRR), NTF2‐like, and UBA modules—enable NXF1 to bind directly to mRNA and interact with FG‐repeat–containing nucleoporins, thereby mediating transit through the nuclear pore complex. Furthermore, during mRNA biogenesis, NXF1 is recruited co‐transcriptionally through interactions with components of the TREX complex (such as Alyref and Chtop), which help drive a conformational “opening” that exposes its RNA‐binding surface and licenses it for export."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "9"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn addition to its pivotal role in cellular mRNA export, NXF1 is frequently exploited by viruses to subvert the host export machinery and ensure efficient viral gene expression. A variety of viral proteins—including the herpes simplex virus ICP27, Kaposi’s sarcoma–associated herpesvirus ORF57, varicella‐zoster virus IE4, influenza A virus factors, hepatitis B virus core protein, Ebola virus nucleoprotein, and even modulators linked to neurodegeneration—directly interact with NXF1 or its cofactors. These interactions tether viral transcripts to the export receptor, thereby promoting their transit from the nucleus into the cytoplasm and contributing to viral propagation."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "10", "end_ref": "20"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its classic role in mRNA export, NXF1 is intricately involved in broader layers of post‐transcriptional regulation. It helps modulate alternative polyadenylation and influences the nuclear retention of select transcripts (for example, contributing to the retention of the long noncoding RNA XIST), thereby affecting mRNA stability and expression profiles. Structural and biochemical studies have revealed features such as oligomerization and multiple, sometimes redundant, nuclear import pathways that fine‐tune NXF1’s activity. In addition, emerging work highlights its interplay with factors like CDK12 and m^6A readers in coupling mRNA export to transcriptional control. Genetic variation in the TAP/NXF1 gene has also been linked to altered immune responses and increased susceptibility to infectious diseases, demonstrating its importance in both health and disease."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "21", "end_ref": "31"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Dona N Ho, Glen A Coburn, Yibin Kang, et al. 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