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• W2744293876 startingPage "861" @default.
• W2744293876 abstract "Xpo1p (yeast CRM 1) is the major nuclear export receptor that carries a plethora of proteins and ribonucleoproteins from the nucleus to cytoplasm. The passage of the Xpo1p nuclear export complex through nuclear pore complexes ( NPC s) is facilitated by interactions with nucleoporins (Nups) containing extensive repeats of phenylalanine–glycine (so‐called FG repeats), although the precise role of each Nup in the nuclear export reaction remains incompletely understood. Here we report structural and biochemical characterization of the interactions between the Xpo1p nuclear export complex and the FG repeats of Nup42p, a nucleoporin localized at the cytoplasmic face of yeast NPC s and has characteristic Sx FG /Px FG sequence repeat motif. The crystal structure of Xpo1p‐ PKI ‐Nup42p‐Gsp1p‐ GTP complex identified three binding sites for the Sx FG /Px FG repeats on HEAT repeats 14–20 of Xpo1p. Mutational analyses of Nup42p showed that the conserved serines and prolines in the Sx FG /Px FG repeats contribute to Xpo1p‐Nup42p binding. Our structural and biochemical data suggest that Sx FG /Px FG ‐Nups such as Nup42p and Nup159p at the cytoplasmic face of NPC s provide high‐affinity docking sites for the Xpo1p nuclear export complex in the terminal stage of NPC passage and that subsequent disassembly of the nuclear export complex facilitates recycling of free Xpo1p back to the nucleus." @default.
• W2744293876 created "2017-08-17" @default.
• W2744293876 creator A5022576150 @default.
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• W2744293876 date "2017-08-08" @default.
• W2744293876 modified "2023-10-01" @default.
• W2744293876 title "Crystal structure of the Xpo1p nuclear export complex bound to the SxFG/PxFG repeats of the nucleoporin Nup42p" @default.
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• W2744293876 doi "https://doi.org/10.1111/gtc.12520" @default.
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