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Architecture of the fungal nuclear pore inner ring complex

by Lin, Daniel H. , Petrovic, Stefan , Kossiakoff, Anthony A. , Schilbach, Sandra , Perriches, Thibaud , Bley, Christopher J. , Collins, Leslie N. , Thierbach, Karsten , Hurt, Ed , Koide, Akiko , Hoelz, André , Mayo, Daniel J. , Fischer, Jessica , Stuwe, Tobias , Jeon, Young E. , Lu, Vincent , Paduch, Marcin , Rundlet, Emily J. , Koide, Shohei , Huber, Ferdinand M.

in Amino Acid Sequence / Architecture / Chaetomium - metabolism / Chaetomium - ultrastructure / Channels / Cytoplasm / Diffusion barriers / Fungal Proteins - chemistry / Fungal Proteins - ultrastructure / Fungi / Metazoa / Molecular Sequence Data / Nuclear Pore - metabolism / Nuclear Pore - ultrastructure / Nuclear Pore Complex Proteins - chemistry / Nuclear Pore Complex Proteins - ultrastructure / Nuclear power generation / Nuclear Proteins - chemistry / Nuclear Proteins - ultrastructure / Nuclei / Porosity / Protein Binding / Protein Multimerization / Protein Structure, Secondary / Protein Structure, Tertiary / Proteins / RESEARCH ARTICLE / Transport

2015

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Architecture of the fungal nuclear pore inner ring complex

2015

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2015

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Journal Article

Architecture of the fungal nuclear pore inner ring complex

Lin, Daniel H.,

Petrovic, Stefan,

Kossiakoff, Anthony A.,

Schilbach, Sandra,

Perriches, Thibaud,

Bley, Christopher J.,

Collins, Leslie N.,

Thierbach, Karsten,

Hurt, Ed,

Koide, Akiko,

Hoelz, André,

Mayo, Daniel J.,

Fischer, Jessica,

Stuwe, Tobias,

Jeon, Young E.,

Lu, Vincent,

Paduch, Marcin,

Rundlet, Emily J.,

Koide, Shohei,

Huber, Ferdinand M.

2015

Overview

The nuclear pore complex (NPC) constitutes the sole gateway for bidirectional nucleocytoplasmic transport. We present the reconstitution and interdisciplinary analyses of the ∼425-kilodalton inner ring complex (IRC), which forms the central transport channel and diffusion barrier of the NPC, revealing its interaction network and equimolar stoichiometry. The Nsp1•Nup49•Nup57 channel nucleoporin heterotrimer (CNT) attaches to the IRC solely through the adaptor nucleoporin Nic96. The CNT•Nic96 structure reveals that Nic96 functions as an assembly sensor that recognizes the three-dimensional architecture of the CNT, thereby mediating the incorporation of a defined CNT state into the NPC. We propose that the IRC adopts a relatively rigid scaffold that recruits the CNT to primarily form the diffusion barrier of the NPC, rather than enabling channel dilation.

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Publisher

American Association for the Advancement of Science,The American Association for the Advancement of Science,AAAS

Subject

Amino Acid Sequence

/ Architecture

/ Chaetomium - metabolism

/ Chaetomium - ultrastructure

/ Channels

/ Cytoplasm

/ Diffusion barriers