{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nNUP153 is a key nucleoporin whose dynamic FG‐rich domains critically regulate nucleocytoplasmic trafficking and nuclear pore complex (NPC) assembly. Studies have revealed that its flexible FG repeat regions can adopt distinct conformations upon binding transport receptors such as karyopherin‐β1, with Ran GTPase modulating these conformational states to allow selective cargo passage. In addition, its N‐terminal amphipathic helix is essential for binding the inner nuclear membrane and recruiting the Nup107–160 complex to facilitate interphase NPC assembly, while its rapid exchange at the pore under transcriptional control hints at additional regulatory roles in nucleocytoplasmic transport and NPC remodeling."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "5"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its classical transport function, NUP153 has emerged as an important regulator of gene expression and genome maintenance. It directly interacts with transcription factors such as Smad2, thereby modulating nucleocytoplasmic shuttling and influencing TGFβ‐mediated signaling. In Drosophila, Nup153 associates with chromatin‐regulatory MSL complexes to ensure proper dosage compensation, while it also governs the nuclear import of key DNA damage response mediators including 53BP1. These interactions, which are mediated through competitive binding at specific hydrophobic interfaces, underline its role in coordinating transcriptional control and efficient DNA repair."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "6", "end_ref": "11"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nNUP153 is also exploited by various viruses as a gateway for nuclear entry. Lentiviruses such as HIV‐1 and EIAV, as well as retroviruses and even certain papillomaviruses, engage the FG motifs of NUP153 to mediate the nuclear import of their reverse transcribed genomes or viral proteins. Direct interactions between viral capsids or proteins (e.g., integrase, Vpr, and HPV E7) and discrete FG‐containing regions of NUP153 have been shown to determine infection efficiency, integration site selection, and the ability to infect nondividing cells. Thus, NUP153 represents a critical host factor that many viruses commandeer to traverse the NPC and establish infection."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "12", "end_ref": "20"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn addition to its roles in transport and viral pathogenesis, NUP153 is vital for maintaining nuclear integrity during cell division and under various stress conditions. Its function in ensuring proper mitotic progression is underscored by studies showing that reduced levels of NUP153 delay late‐stage mitosis and disrupt cytokinesis. By directly engaging with nuclear lamins and other components of the nuclear basket—and through interactions with regulators such as importin‐α and RTEL1—it helps preserve nuclear envelope stability and modulate nuclear import under conditions of oxidative stress. Such functions not only impact normal cell cycle progression but also have been implicated in human diseases, including cardiomyopathy, hepatocellular carcinoma, and neurodegeneration."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "21", "end_ref": "32"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Eric R Griffis, Branch Craige, Christian Dimaano, et al. 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