Comprehensive structure and functional adaptations of the yeast nuclear pore complex.
Adaptation, Physiological
Amino Acid Motifs
Amino Acid Sequence
Fluorescence
Molecular Docking Simulation
Nuclear Envelope
/ metabolism
Nuclear Pore
/ chemistry
Nuclear Pore Complex Proteins
/ chemistry
Protein Domains
Reproducibility of Results
Saccharomyces cerevisiae
/ physiology
Saccharomyces cerevisiae Proteins
/ chemistry
NPC evolution
Nuclear pore complex
cryo-electron microscopy
cryo-electron tomography
inner ring dilation
nuclear basket
nucleocytoplasmic transport
nucleoporins
structural isoforms
Journal
Cell
ISSN: 1097-4172
Titre abrégé: Cell
Pays: United States
ID NLM: 0413066
Informations de publication
Date de publication:
20 01 2022
20 01 2022
Historique:
received:
29
06
2021
revised:
26
11
2021
accepted:
13
12
2021
pubmed:
5
1
2022
medline:
23
2
2022
entrez:
4
1
2022
Statut:
ppublish
Résumé
Nuclear pore complexes (NPCs) mediate the nucleocytoplasmic transport of macromolecules. Here we provide a structure of the isolated yeast NPC in which the inner ring is resolved by cryo-EM at sub-nanometer resolution to show how flexible connectors tie together different structural and functional layers. These connectors may be targets for phosphorylation and regulated disassembly in cells with an open mitosis. Moreover, some nucleoporin pairs and transport factors have similar interaction motifs, which suggests an evolutionary and mechanistic link between assembly and transport. We provide evidence for three major NPC variants that may foreshadow functional specializations at the nuclear periphery. Cryo-electron tomography extended these studies, providing a model of the in situ NPC with a radially expanded inner ring. Our comprehensive model reveals features of the nuclear basket and central transporter, suggests a role for the lumenal Pom152 ring in restricting dilation, and highlights structural plasticity that may be required for transport.
Identifiants
pubmed: 34982960
pii: S0092-8674(21)01453-7
doi: 10.1016/j.cell.2021.12.015
pmc: PMC8928745
mid: NIHMS1767905
pii:
doi:
Substances chimiques
Nuclear Pore Complex Proteins
0
Saccharomyces cerevisiae Proteins
0
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.
Langues
eng
Sous-ensembles de citation
IM
Pagination
361-378.e25Subventions
Organisme : NIGMS NIH HHS
ID : R01 GM080139
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM083960
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM112108
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM117212
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM045377
Pays : United States
Organisme : NIGMS NIH HHS
ID : DP2 GM123494
Pays : United States
Organisme : NIGMS NIH HHS
ID : P41 GM109824
Pays : United States
Commentaires et corrections
Type : CommentIn
Informations de copyright
Copyright © 2021 The Authors. Published by Elsevier Inc. All rights reserved.
Déclaration de conflit d'intérêts
Declaration of interests The authors declare no competing interests.
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