Structure and gating of the nuclear pore complex

Eibauer, Matthias; Pellanda, Mauro; Turgay, Yagmur; Dubrovsky, Anna; Wild, Arie de; Medalia, Ohad

doi:10.1038/ncomms8532

Cited by 178 publications

(223 citation statements)

References 49 publications

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“…Fourth, the structure was also validated by its comparison to the core scaffold maps of the Homo sapiens NPC, based primarily on EM density maps 79,80,140,141 (Extended Data Fig. 10).…”

Section: Methodsmentioning

confidence: 99%

Integrative structure and functional anatomy of a nuclear pore complex

Kim

Fernández-Martı́nez

Nudelman

et al. 2018

Nature

478

894

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Summary Despite the central role of Nuclear Pore Complexes (NPCs) as gatekeepers of RNA and protein transport between the cytoplasm and nucleoplasm, their large size and dynamic nature have impeded a full structural and functional elucidation. Here, we have determined a subnanometer precision structure for the entire 552-protein yeast NPC by satisfying diverse data including stoichiometry, a cryo-electron tomography map, and chemical cross-links. The structure reveals the NPC’s functional elements in unprecedented detail. The NPC is built of sturdy diagonal columns to which are attached connector cables, imbuing both strength and flexibility, while tying together all other elements of the NPC, including membrane-interacting regions and RNA processing platforms. Inwardly-directed anchors create a high density of transport factor-docking Phe-Gly repeats in the central channel, organized in distinct functional units. Taken together, this integrative structure allows us to rationalize the architecture, transport mechanism, and evolutionary origins of the NPC.

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“…Fourth, the structure was also validated by its comparison to the core scaffold maps of the Homo sapiens NPC, based primarily on EM density maps 79,80,140,141 (Extended Data Fig. 10).…”

Section: Methodsmentioning

confidence: 99%

Integrative structure and functional anatomy of a nuclear pore complex

Kim

Fernández-Martı́nez

Nudelman

et al. 2018

Nature

478

894

View full text Add to dashboard Cite

show abstract

“…Indeed, such a picture is consistent with the preferred localization of Kapb1 in the NPC as observed in single molecule fluorescence experiments, 60,61 as well as structural changes inside the central channel as revealed by cryo-electron tomography. 62 Fast transport kinetics would then emerge from a culmination of 3 effects along this corridor: (i) reduced Kap-FG repeat binding, (ii) ROD, and (iii) spatial confinement.…”

Section: Implications Of Kap-centric Controlmentioning

confidence: 99%

How to operate a nuclear pore complex by Kap-centric control

Lim

Huang

Kapinos

2015

Nucleus

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“…77 The native structure of the nucleocytoplasmic barrier has been visualized: the central channel is occupied by an ordered structure of high-density, which appears to be a ring-like assembly physically attached to the spokering with a porous interface approximately 23 nm from the central channel pore axial. Furthermore, the central channel ring also links extends to the cytoplasmic ring and the entangled filamentous nucleoplasmic ring.…”

Section: Computational Simulation Cryo-em and Speed Microscopy In Fgmentioning

confidence: 99%

The selective permeability barrier in the nuclear pore complex

Goryaynov

Yang

2016

Nucleus

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The nuclear pore complex (NPC) mediates the shuttle transport of macromolecules between the nucleus and cytoplasm in eukaryotic cells. The permeability barrier formed by intrinsically disordered phenylalanine-glycine-rich nucleoporins (FG-Nups) in the NPC functions as the critical selective control for nucleocytoplasmic transport. Signal-independent small molecules (< 40 kDa) passively diffuse through the pore, but passage of large cargo molecules is inhibited unless they are chaperoned by nuclear transport receptors (NTRs). NTRs are capable of interacting with FG-Nups and guide the cargos to cross the barrier by facilitated diffusion. The native conformation of the FGNups permeability barrier and the competition among multiple NTRs interacting with this barrier in the native NPCs are the 2 core questions still being highly debated in the field. Recently, we applied high-speed super-resolution fluorescence microscopy to map out the natural structure of the FGNups barrier and determined the competition among multiple NTRs as they interact with the barrier in the native NPCs. In this extra-view article, we will review the current understanding in the configuration and function of FG-Nups barrier and highlight the new evidence obtained recently to answer the core questions in nucleocytoplasmic transport.

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Structure and gating of the nuclear pore complex

Cited by 178 publications

References 49 publications

Integrative structure and functional anatomy of a nuclear pore complex

Integrative structure and functional anatomy of a nuclear pore complex

How to operate a nuclear pore complex by Kap-centric control

The selective permeability barrier in the nuclear pore complex

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