Department:Massachusetts Institute of Technology. Dept. of Biology
Publisher:Nature Publishing Group
Date Issued:2009-10
Abstract:
Nuclear pore complexes (NPCs) facilitate all nucleocytoplasmic transport. These massive protein assemblies are modular, with a stable structural scaffold supporting more dynamically attached components. The scaffold is made from multiple copies of the heptameric Y complex and the heteromeric Nic96 complex. We previously showed that members of these core subcomplexes specifically share an ACE1 fold with Sec31 of the COPII vesicle coat, and we proposed a lattice model for the NPC based on this commonality. Here we present the crystal structure of the heterotrimeric 134-kDa complex of Nup84–Nup145C–Sec13 of the Y complex. The heterotypic ACE1 interaction of Nup84 and Nup145C is analogous to the homotypic ACE1 interaction of Sec31 that forms COPII lattice edge elements and is inconsistent with the alternative 'fence-like' NPC model. We construct a molecular model of the Y complex and compare the architectural principles of COPII and NPC lattices.
Citation:Brohawn, Stephen G, and Thomas U Schwartz. “Molecular Architecture of the Nup84–Nup145C–Sec13 Edge Element in the Nuclear Pore Complex Lattice.” Nature Structural & Molecular Biology 16.11 (2009): 1173–1177.
Version:Author's final manuscript
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