Nuclear Pores Assemble from Nucleoporin Condensates During Oogenesis.


Journal

Cell
ISSN: 1097-4172
Titre abrégé: Cell
Pays: United States
ID NLM: 0413066

Informations de publication

Date de publication:
17 10 2019
Historique:
received: 20 11 2018
revised: 09 08 2019
accepted: 20 09 2019
entrez: 19 10 2019
pubmed: 19 10 2019
medline: 28 5 2020
Statut: ppublish

Résumé

The molecular events that direct nuclear pore complex (NPC) assembly toward nuclear envelopes have been conceptualized in two pathways that occur during mitosis or interphase, respectively. In gametes and embryonic cells, NPCs also occur within stacked cytoplasmic membrane sheets, termed annulate lamellae (AL), which serve as NPC storage for early development. The mechanism of NPC biogenesis at cytoplasmic membranes remains unknown. Here, we show that during Drosophila oogenesis, Nucleoporins condense into different precursor granules that interact and progress into NPCs. Nup358 is a key player that condenses into NPC assembly platforms while its mRNA localizes to their surface in a translation-dependent manner. In concert, Microtubule-dependent transport, the small GTPase Ran and nuclear transport receptors regulate NPC biogenesis in oocytes. We delineate a non-canonical NPC assembly mechanism that relies on Nucleoporin condensates and occurs away from the nucleus under conditions of cell cycle arrest.

Identifiants

pubmed: 31626769
pii: S0092-8674(19)31073-6
doi: 10.1016/j.cell.2019.09.022
pmc: PMC6838685
pii:
doi:

Substances chimiques

Drosophila Proteins 0
Molecular Chaperones 0
Nuclear Pore Complex Proteins 0
RNA, Messenger 0
ran-binding protein 2 0
ran GTP-Binding Protein EC 3.6.5.2

Types de publication

Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

671-686.e17

Subventions

Organisme : NIH HHS
ID : P40 OD018537
Pays : United States

Commentaires et corrections

Type : CommentIn
Type : CommentIn
Type : CommentIn

Informations de copyright

Copyright © 2019 The Authors. Published by Elsevier Inc. All rights reserved.

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Auteurs

Bernhard Hampoelz (B)

European Molecular Biology Laboratory, Structural and Computational Biology Unit, Heidelberg, Germany; Max Planck Institute of Biophysics, Frankfurt am Main, Germany. Electronic address: bernhard.hampoelz@embl.de.

Andre Schwarz (A)

European Molecular Biology Laboratory, Structural and Computational Biology Unit, Heidelberg, Germany; Collaboration for joint PhD degree between EMBL and Heidelberg University, Faculty of Biosciences.

Paolo Ronchi (P)

European Molecular Biology Laboratory, Electron Microscopy Core Facility, Heidelberg, Germany.

Helena Bragulat-Teixidor (H)

European Molecular Biology Laboratory, Electron Microscopy Core Facility, Heidelberg, Germany.

Christian Tischer (C)

Center for Bioimage Analysis, European Molecular Biology Laboratory, Heidelberg, Germany.

Imre Gaspar (I)

European Molecular Biology Laboratory, Developmental Biology Unit, Heidelberg, Germany.

Anne Ephrussi (A)

European Molecular Biology Laboratory, Developmental Biology Unit, Heidelberg, Germany.

Yannick Schwab (Y)

European Molecular Biology Laboratory, Electron Microscopy Core Facility, Heidelberg, Germany; European Molecular Biology Laboratory, Cell Biology and Biophysics Unit, Heidelberg, Germany.

Martin Beck (M)

European Molecular Biology Laboratory, Structural and Computational Biology Unit, Heidelberg, Germany; Max Planck Institute of Biophysics, Frankfurt am Main, Germany; European Molecular Biology Laboratory, Cell Biology and Biophysics Unit, Heidelberg, Germany. Electronic address: martin.beck@biophys.mpg.de.

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Classifications MeSH