Structure and gating of the nuclear pore complex

Matthias Eibauer; Mauro Pellanda; Yagmur Turgay; Anna Dubrovsky; Annik Wild; Ohad Medalia

doi:10.1038/ncomms8532

Structure and gating of the nuclear pore complex

Matthias Eibauer, Mauro Pellanda, Yagmur Turgay, Anna Dubrovsky, Annik Wild, Ohad Medalia

Department of Life Sciences

Research output: Contribution to journal › Article › peer-review

142 Scopus citations

Abstract

Nuclear pore complexes (NPCs) perforate the nuclear envelope and allow the exchange of macromolecules between the nucleus and the cytoplasm. To acquire a deeper understanding of this transport mechanism, we analyse the structure of the NPC scaffold and permeability barrier, by reconstructing the Xenopus laevis oocyte NPC from native nuclear envelopes up to 20â €‰Å resolution by cryo-electron tomography in conjunction with subtomogram averaging. In addition to resolving individual protein domains of the NPC constituents, we propose a model for the architecture of the molecular gate at its central channel. Furthermore, we compare and contrast this native NPC structure to one that exhibits reduced transport activity and unveil the spatial properties of the NPC gate.

Original language	English
Article number	7532
Journal	Nature Communications
Volume	6
DOIs	https://doi.org/10.1038/ncomms8532
State	Published - 26 Jun 2015

ASJC Scopus subject areas

General Chemistry
General Biochemistry, Genetics and Molecular Biology
General Physics and Astronomy

Access to Document

10.1038/ncomms8532

Cite this

@article{c06405bbe745483b9fa09cd717c80f36,

title = "Structure and gating of the nuclear pore complex",

abstract = "Nuclear pore complexes (NPCs) perforate the nuclear envelope and allow the exchange of macromolecules between the nucleus and the cytoplasm. To acquire a deeper understanding of this transport mechanism, we analyse the structure of the NPC scaffold and permeability barrier, by reconstructing the Xenopus laevis oocyte NPC from native nuclear envelopes up to 20{\^a} €‰{\AA} resolution by cryo-electron tomography in conjunction with subtomogram averaging. In addition to resolving individual protein domains of the NPC constituents, we propose a model for the architecture of the molecular gate at its central channel. Furthermore, we compare and contrast this native NPC structure to one that exhibits reduced transport activity and unveil the spatial properties of the NPC gate.",

author = "Matthias Eibauer and Mauro Pellanda and Yagmur Turgay and Anna Dubrovsky and Annik Wild and Ohad Medalia",

note = "Funding Information: This work was supported by a Swiss National Science Foundation grant (SNSF 31003A_141083/1) and the Maexi foundation. We would like to thank the Center for Microscopy and Image Analysis of the University of Zurich and Dr Tanuj Sapra and Dr Rossitza Irobalieva for critical reading of the manuscript.",

year = "2015",

month = jun,

day = "26",

doi = "10.1038/ncomms8532",

language = "English",

volume = "6",

journal = "Nature Communications",

issn = "2041-1723",

publisher = "Nature Research",

}

TY - JOUR

T1 - Structure and gating of the nuclear pore complex

AU - Eibauer, Matthias

AU - Pellanda, Mauro

AU - Turgay, Yagmur

AU - Dubrovsky, Anna

AU - Wild, Annik

AU - Medalia, Ohad

N1 - Funding Information: This work was supported by a Swiss National Science Foundation grant (SNSF 31003A_141083/1) and the Maexi foundation. We would like to thank the Center for Microscopy and Image Analysis of the University of Zurich and Dr Tanuj Sapra and Dr Rossitza Irobalieva for critical reading of the manuscript.

PY - 2015/6/26

Y1 - 2015/6/26

N2 - Nuclear pore complexes (NPCs) perforate the nuclear envelope and allow the exchange of macromolecules between the nucleus and the cytoplasm. To acquire a deeper understanding of this transport mechanism, we analyse the structure of the NPC scaffold and permeability barrier, by reconstructing the Xenopus laevis oocyte NPC from native nuclear envelopes up to 20â €‰Å resolution by cryo-electron tomography in conjunction with subtomogram averaging. In addition to resolving individual protein domains of the NPC constituents, we propose a model for the architecture of the molecular gate at its central channel. Furthermore, we compare and contrast this native NPC structure to one that exhibits reduced transport activity and unveil the spatial properties of the NPC gate.

AB - Nuclear pore complexes (NPCs) perforate the nuclear envelope and allow the exchange of macromolecules between the nucleus and the cytoplasm. To acquire a deeper understanding of this transport mechanism, we analyse the structure of the NPC scaffold and permeability barrier, by reconstructing the Xenopus laevis oocyte NPC from native nuclear envelopes up to 20â €‰Å resolution by cryo-electron tomography in conjunction with subtomogram averaging. In addition to resolving individual protein domains of the NPC constituents, we propose a model for the architecture of the molecular gate at its central channel. Furthermore, we compare and contrast this native NPC structure to one that exhibits reduced transport activity and unveil the spatial properties of the NPC gate.

UR - http://www.scopus.com/inward/record.url?scp=84933556640&partnerID=8YFLogxK

U2 - 10.1038/ncomms8532

DO - 10.1038/ncomms8532

M3 - Article

AN - SCOPUS:84933556640

SN - 2041-1723

VL - 6

JO - Nature Communications

JF - Nature Communications

M1 - 7532

ER -

Structure and gating of the nuclear pore complex

Abstract

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this