Structural basis for assembly and function of the Nup82 complex in the nuclear pore scaffold

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  • Nuclear pore complexes (NPCs) are huge assemblies formed from ~30 different nucleoporins, typically organized in subcomplexes. One module, the conserved Nup82 complex at the cytoplasmic face of NPCs, is crucial to terminate mRNA export. To gain insight into the structure, assembly, and function of the cytoplasmic pore filaments, we reconstituted in yeast the Nup82–Nup159–Nsp1–Dyn2 complex, which was suitable for biochemical, biophysical, and electron microscopy analyses. Our integrative approach revealed that the yeast Nup82 complex forms an unusual asymmetric structure with a dimeric array of subunits. Based on all these data, we developed a three-dimensional structural model of the Nup82 complex that depicts how this module might be anchored to the NPC scaffold and concomitantly can interact with the soluble nucleocytoplasmic transport machinery.
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  • Gaik, M., Flemming, D., von Appen, A., Kastritis, P., Mücke, N., Fischer, J., ... & Hurt, E. (2015). Structural basis for assembly and function of the Nup82 complex in the nuclear pore scaffold. Journal of Cell Biology, 208(3), 283-297. doi:10.1083/jcb.201411003
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  • 208
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  • 3
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  • E. Hurt and D. Flemming are recipients of grants from the Deutsche Forschungsgemeinschaft (SFB 638/B2). K.H. Bui was supported by postdoctoral fellowships from the Swiss National Science Foundation, the European Molecular Biology Organization, and Marie Curie Actions. M. Beck acknowledges funding by the European Research Council (309271-NPC Atlas). This work was supported by National Institutes of Health grant GM 084276to E. Barbar.
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