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Nucleoporin NUP42 is a conserved component of the cytoplasmic face of the nuclear pore complex (NPC). It participates in mRNA export by providing FG-repeat domains that facilitate mRNP remodeling and interact with transport and processing factors such as Gle1 and Dbp5 at the cytoplasmic end of the NPC. The CTD (C-terminal domain) of NUP42 is required to anchor Gle1 to the NPC, influencing efficient export and remodeling of mRNA particles. NUP42 forms part of the cytoplasmic filament subcomplex contributing to the flexible structure and transport activities of the NPC, notably facilitating the final steps of mRNA export, remodeling, and recycling of transport factors[1][2][3][4].\n\nKey references for further structure and function:\n- NUP42 helps recruit mRNA transport and remodeling machinery and is necessary for efficient mRNA export out of the nucleus[1][2][3].\n- Its FG-repeat domain interacts with proteins involved in remodeling exported mRNAs, and its function is tightly linked to Gle1-mediated activation of the DEAD-box helicase Dbp5 for remodeling of mRNPs at the cytoplasmic side of the NPC[3].\n- Disease associations are rare, but mutations in NPC subunits generally contribute to defects in nuclear transport and have secondary roles in cancer and neurodegeneration; however, data implicating NUP42 directly is limited[1][2][4].
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