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Title: Architecture of the nuclear pore complex coat

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Publication Date:
Research Org.:
Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Sponsoring Org.:
OSTI Identifier:
Resource Type:
Journal Article
Resource Relation:
Journal Name: Science; Journal Volume: 347; Journal Issue: 03, 2015
Country of Publication:
United States

Citation Formats

Stuwe, Tobias, Correia, Ana R., Lin, Daniel H., Paduch, Marcin, Lu, Vincent T., Kossiakoff, Anthony A., Hoelz, André, and CIT). Architecture of the nuclear pore complex coat. United States: N. p., 2016. Web. doi:10.1126/science.aaa4136.
Stuwe, Tobias, Correia, Ana R., Lin, Daniel H., Paduch, Marcin, Lu, Vincent T., Kossiakoff, Anthony A., Hoelz, André, & CIT). Architecture of the nuclear pore complex coat. United States. doi:10.1126/science.aaa4136.
Stuwe, Tobias, Correia, Ana R., Lin, Daniel H., Paduch, Marcin, Lu, Vincent T., Kossiakoff, Anthony A., Hoelz, André, and CIT). 2016. "Architecture of the nuclear pore complex coat". United States. doi:10.1126/science.aaa4136.
title = {Architecture of the nuclear pore complex coat},
author = {Stuwe, Tobias and Correia, Ana R. and Lin, Daniel H. and Paduch, Marcin and Lu, Vincent T. and Kossiakoff, Anthony A. and Hoelz, André and CIT)},
abstractNote = {},
doi = {10.1126/science.aaa4136},
journal = {Science},
number = 03, 2015,
volume = 347,
place = {United States},
year = 2016,
month = 6
  • The symmetric core of the nuclear pore complex can be considered schematically as a series of concentric cylinders. A peripheral cylinder coating the pore membrane contains the previously characterized, elongated heptamer that harbors Sec13-Nup145C in its middle section. Strikingly, Sec13-Nup145C crystallizes as a hetero-octamer in two space groups. Oligomerization of Sec13-Nup145C was confirmed biochemically. Importantly, the numerous interacting surfaces in the hetero-octamer are evolutionarily highly conserved, further underlining the physiological relevance of the oligomerization. The hetero-octamer forms a slightly curved, yet rigid rod of sufficient length to span the entire height of the proposed membrane-adjacent cylinder. In concordance with themore » dimensions and symmetry of the nuclear pore complex core, we suggest that the cylinder is constructed of four antiparallel rings, each ring being composed of eight heptamers arranged in a head-to-tail fashion. Our model proposes that the hetero-octamer would vertically traverse and connect the four stacked rings.« less
  • 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 Nup145Cmore » 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.« less
  • Nuclear pore complexes (NPCs) are 4060 MDa protein assemblies embedded in the nuclear envelope of eukaryotic cells. NPCs exclusively mediate all transport between cytoplasm and nucleus. The nucleoporins that build the NPC are arranged in a stable core of module-like subcomplexes with eight-fold rotational symmetry. To gain insight into the intricate assembly of the NPC, we have solved the crystal structure of a protein complex between two nucleoporins, human Nup107 and Nup133. Both proteins form elongated structures that interact tightly via a compact interface in tail-to-tail fashion. Additional experiments using structure-guided mutants show that Nup107 is the critical anchor formore » Nup133 to the NPC, positioning Nup133 at the periphery of the NPC. The significant topological differences between Nup107 and Nup133 suggest that {alpha}-helical nucleoporin domains of the NPC scaffold fall in different classes and fulfill largely nonredundant functions.« less
  • The nuclear pore complex encloses a central channel for nucleocytoplasmic transport, which is thought to consist of three nucleoporins, Nup54, Nup58, and Nup62. However, the structure and composition of the channel are elusive. We determined the crystal structures of the interacting domains between these nucleoporins and pieced together the molecular architecture of the mammalian transport channel. Located in the channel midplane is a flexible Nup54Nup58 ring that can undergo large rearrangements yielding diameter changes from {approx}20 to {approx}40 nm. Nup62Nup54 triple helices project alternately up and down from either side of the midplane ring and form nucleoplasmic and cytoplasmic entries.more » The channel consists of as many as 224 copies of the three nucleoporins, amounting to a molar mass of 12.3 MDa and contributing 256 phenylalanine-glycine repeat regions. We propose that the occupancy of these repeat regions with transport receptors modulates ring diameter and transport activity.« less