| Autor: |
Daniel Zenklusen, Javier Fernandez-Martinez, Michael P. Rout, Wenzhu Zhang, Paula Upla, Rosemary Williams, Brian T. Chait, David L. Stokes, Michael Gagnon, Seung Joong Kim, Andrej Sali, Yi Shi, Ilan E. Chemmama, Riccardo Pellarin, Ilona Nudelman, William J. Rice, Junjie Wang |
| Rok vydání: |
2016 |
| Předmět: |
|
| Zdroj: |
Cell, vol 167, iss 5 |
| Popis: |
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 compositionallyidentical 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 ondistal cytoplasmic filaments, as previously supposed. We suggest that this configuration efficiently captures and remodels exporting mRNP particles immediately upon reaching the cytoplasmic side ofthe NPC. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
|
