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  In-cell architecture of the nuclear pore and snapshots of its turnover

Allegretti, M., Zimmerli, C. E., Rantos, V., Wilfling, F., Ronchi, P., Fung, H. K. H., et al. (2020). In-cell architecture of the nuclear pore and snapshots of its turnover. Nature. doi:10.1038/s41586-020-2670-5.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0007-14B7-4 Version Permalink: http://hdl.handle.net/21.11116/0000-0007-14B8-3
Genre: Journal Article

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https://rdcu.be/b7NK6 (Publisher version)
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 Creators:
Allegretti, Matteo1, Author
Zimmerli, Christian E.1, Author
Rantos, Vasileios1, Author
Wilfling, Florian2, Author              
Ronchi, Paolo1, Author
Fung, Herman K. H.1, Author
Lee, Chia-Wei2, Author              
Hagen, Wim1, Author
Turonova, Beata1, Author
Karius, Kai1, Author
Boermel, Mandy1, Author
Zhang, Xiaojie1, Author
Mueller, Christoph W.1, Author
Schwab, Yannick1, Author
Mahamid, Julia1, Author
Pfander, Boris2, Author              
Kosinski, Jan1, Author
Beck, Martin1, Author
Affiliations:
1external, ou_persistent22              
2Jentsch, Stefan / Molecular Cell Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565156              

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Free keywords: MESSENGER-RNA EXPORT; INTEGRATIVE STRUCTURE; CYTOPLASMIC FACE; BINDING-SITES; INNER RING; COMPLEX; ENVELOPE; VISUALIZATION; RESOLUTION; SOFTWAREScience & Technology - Other Topics;
 Abstract: In-cell structural studies inSaccharomyces cerevisiaereveal that the configuration of the Nup159 complex is a key determinant of the mRNA export function of the nuclear pore complex, and suggest a model in which nuclear pore complexes are degraded via the autophagy machinery. Nuclear pore complexes (NPCs) fuse the inner and outer membranes of the nuclear envelope. They comprise hundreds of nucleoporins (Nups) that assemble into multiple subcomplexes and form large central channels for nucleocytoplasmic exchange(1,2). How this architecture facilitates messenger RNA export, NPC biogenesis and turnover remains poorly understood. Here we combine in situ structural biology and integrative modelling with correlative light and electron microscopy and molecular perturbation to structurally analyse NPCs in intactSaccharomyces cerevisiaecells within the context of nuclear envelope remodelling. We find an in situ conformation and configuration of the Nup subcomplexes that was unexpected from the results of previous in vitro analyses. The configuration of the Nup159 complex appears critical to spatially accommodate its function as an mRNA export platform, and as a mediator of NPC turnover. The omega-shaped nuclear envelope herniae that accumulate innup116 Delta cells(3)conceal partially assembled NPCs lacking multiple subcomplexes, including the Nup159 complex. Under conditions of starvation, herniae of a second type are formed that cytoplasmically expose NPCs. These results point to a model of NPC turnover in which NPC-containing vesicles bud off from the nuclear envelope before degradation by the autophagy machinery. Our study emphasizes the importance of investigating the structure-function relationship of macromolecular complexes in their cellular context.

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Language(s): eng - English
 Dates: 2020-09-02
 Publication Status: Published online
 Pages: 27
 Publishing info: -
 Table of Contents: -
 Rev. Type: -
 Identifiers: ISI: 000565516400007
DOI: 10.1038/s41586-020-2670-5
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Project name : EMBO Long-Term Fellowship ALTF 764-2014
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Title: Nature
  Abbreviation : Nature
Source Genre: Journal
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Publ. Info: London : Nature Publishing Group
Pages: - Volume / Issue: - Sequence Number: - Start / End Page: - Identifier: ISSN: 0028-0836
CoNE: https://pure.mpg.de/cone/journals/resource/954925427238