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Nucleoporin GLE1 is a conserved protein essential for the terminal step in nuclear export of polyadenylated (poly(A)+) mRNA through the nuclear pore complex (NPC)[1][3]. It functions at the cytoplasmic face of the NPC, interacting with nucleoporins such as NUP155, Nup42, and Nup214, and activates the DEAD-box helicase DDX19, which remodels mRNPs and releases export factors from translocating transcripts[1][2]. Human GLE1 exists as at least two isoforms (GLE1A and GLE1B); the latter specifically localizes at the NPC and plays a critical role in stress response via mRNA export[1][2]. GLE1 exhibits high homology to yeast Gle1 and is pivotal to maintaining efficient gene expression in all eukaryotes. Mutations in GLE1 are associated with severe neurodegenerative diseases such as lethal congenital contracture syndrome, underscoring its biological importance in development and neural function[2][3].
Not applicable; no known drugs directly target GLE1. Inhibition or destabilization of GLE1 can block mRNA export, particularly for stress-induced transcripts (e.g., Hsp70). Modulation of GLE1 could alter interactions with DDX19 and nucleoporins.
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