Abstract
CRM1 (or exportin 1, Xpo1) transports proteins out of the cell nucleus through the nuclear pore complex. In the cytoplasm, GTP hydrolysis and consequent dissociation of Ran from CRM1 releases low-affinity substrates, while additional factors facilitate release of high-affinity substrates. Here we provide a model for human CRM1 export complex assembly and disassembly through structural and biochemical analyses of CRM1 bound to the substrate snurportin 1 (SNUPN, also called snuportin 1).
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Acknowledgements
We thank Q. Jiang for help with EM map analyses and M. Rosen for critical reading of the manuscript. This work is funded by US National Institutes of Health grants R01GM069909, R01GM069909-03S1 and 5-T32-GM008297, Welch Foundation grant I-1532 and the University of Texas Southwestern Endowed Scholars Program. Use of the Argonne National Laboratory Structural Biology Center beamlines at the Advanced Photon Source was supported by the US Department of Energy, Office of Energy Research, under contract no. W-31-109-ENG-38.
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Dong, X., Biswas, A. & Chook, Y. Structural basis for assembly and disassembly of the CRM1 nuclear export complex. Nat Struct Mol Biol 16, 558–560 (2009). https://doi.org/10.1038/nsmb.1586
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DOI: https://doi.org/10.1038/nsmb.1586
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