| Literature DB >> 27839866 |
Javier Fernandez-Martinez1, Seung Joong Kim2, Yi Shi3, Paula Upla4, Riccardo Pellarin5, Michael Gagnon6, Ilan E Chemmama2, Junjie Wang3, Ilona Nudelman1, Wenzhu Zhang3, Rosemary Williams1, William J Rice7, David L Stokes4, Daniel Zenklusen6, Brian T Chait8, Andrej Sali9, Michael P Rout10.
Abstract
The last steps in mRNA export and remodeling are performed by the Nup82 complex, a large conserved assembly at the cytoplasmic face of the nuclear pore complex (NPC). By integrating diverse structural data, we have determined the molecular architecture of the native Nup82 complex at subnanometer precision. The complex consists of two compositionally identical multiprotein subunits that adopt different configurations. The Nup82 complex fits into the NPC through the outer ring Nup84 complex. Our map shows that this entire 14-MDa Nup82-Nup84 complex assembly positions the cytoplasmic mRNA export factor docking sites and messenger ribonucleoprotein (mRNP) remodeling machinery right over the NPC's central channel rather than on distal cytoplasmic filaments, as previously supposed. We suggest that this configuration efficiently captures and remodels exporting mRNP particles immediately upon reaching the cytoplasmic side of the NPC.Entities:
Keywords: Nup4 complex; Nup82 complex; computational structural biology; cross-linking and mass spectrometry; electron microscopy; integrative structure determination; mRNA export; mRNP remodeling; nuclear pore complex; small-angle X-ray scattering
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Year: 2016 PMID： 27839866 PMCID： PMC5130164 DOI： 10.1016/j.cell.2016.10.028
Source DB: PubMed Journal: Cell ISSN： 0092-8674 Impact factor: 41.582