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Molecular architecture of the Nup84–Nup145C–Sec13 edge element in the nuclear pore complex lattice

Nature Structural & Molecular Biology volume 16, pages 1173–1177 (2009)Cite this article

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.

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Figure 1: Structure of Nup84–Nup145C–Sec13.
Figure 2: The crown-crown interaction of Nup84–Nup145C is analogous to that of Sec31–Sec31.
Figure 3: Comparison of edge elements in the NPC and COPII lattices.
Figure 4: Nup84–Nup145C is a membrane curvature–stabilizing edge element in the NPC lattice.

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Acknowledgements

We thank the staff at beamlines 24-ID-C/-E at Argonne National Laboratory for assistance with data collection, the staff at beamline X29 at the National Synchrotron Light Source for assistance in screening cryoprotection conditions through mail-in data collection service, M. Gogala for his contributions to the Nup145C109–179–Sec13 structure, J. Iwasa for help with Figure 4, and members of the Schwartz laboratory for valuable discussions. This work was supported by National Institutes of Health grant GM77537, a Pew Scholar award (to T.U.S.) and a Koch Fellowship (to S.G.B).

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  1. Department of Biology, Massachusetts Institute of Technology, Cambridge, Massachusetts, USA

    Stephen G Brohawn & Thomas U Schwartz

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  1. Stephen G Brohawn
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S.G.B. designed, conducted and analyzed biochemical, biophysical and crystallographic experiments and wrote the manuscript; T.U.S. advised on all aspects of the project and wrote the manuscript.

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Correspondence to Thomas U Schwartz.

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Brohawn, S., Schwartz, T. Molecular architecture of the Nup84–Nup145C–Sec13 edge element in the nuclear pore complex lattice. Nat Struct Mol Biol 16, 1173–1177 (2009). https://doi.org/10.1038/nsmb.1713

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