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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, 586(7831), 796-800. doi:10.1038/s41586-020-2670-5.

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 Creators:
Allegretti, Matteo1, Author
Zimmerli, Christian E.1, 2, Author
Rantos, Vasileios3, Author
Wilfling, Florian4, Author              
Ronchi, Paolo5, Author
Fung, Herman K. H.1, Author
Lee, Chia-Wei6, Author
Hagen, Wim1, Author
Turoňová, Beata1, Author
Karius, Kai3, Author
Börmel, Mandy5, Author
Zhang, Xiaojie1, Author
Müller, Christoph W.1, Author
Schwab, Yannick5, 7, Author
Mahamid, Julia1, 7, Author
Pfander, Boris6, Author
Kosinski, Jan1, 3, Author
Beck, Martin1, 7, 8, Author              
Affiliations:
1Structural and Computational Biology Unit, European Molecular Biology Laboratory (EMBL), Heidelberg, Germany, ou_persistent22              
2Collaboration for joint PhD degree between EMBL and Heidelberg University, Faculty of Biosciences, Heidelberg, Germany, ou_persistent22              
3Centre for Structural Systems Biology (CSSB), DESY and European Molecular Biology Laboratory, Hamburg, Germany, ou_persistent22              
4Jentsch, Stefan / Molecular Cell Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565156              
5Electron Microscopy Core Facility (EMCF), European Molecular Biology Laboratory, Heidelberg, Germany, ou_persistent22              
6Max Planck Institute of Biochemistry, Martinsried, Germany, ou_persistent22              
7Cell Biology and Biophysics Unit, European Molecular Biology Laboratory (EMBL), Heidelberg, Germany, ou_persistent22              
8Department of Molecular Sociology, Max Planck Institute of Biophysics, Max Planck Society, ou_3040395              

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 Abstract: 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 exchange1,2. 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 intact Saccharomyces cerevisiae cells 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 in nup116Δ cells3 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: 2019-08-072020-06-012020-09-022020-10-29
 Publication Status: Published in print
 Pages: 5
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1038/s41586-020-2670-5
BibTex Citekey: allegretti_-cell_2020
 Degree: -

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Title: Nature
  Abbreviation : Nature
Source Genre: Journal
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Publ. Info: London : Nature Publishing Group
Pages: - Volume / Issue: 586 (7831) Sequence Number: - Start / End Page: 796 - 800 Identifier: ISSN: 0028-0836
CoNE: https://pure.mpg.de/cone/journals/resource/954925427238