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TitleIn-cell architecture of the nuclear pore and snapshots of its turnover.
Journal, issue, pagesNature, Vol. 586, Issue 7831, Page 796-800, Year 2020
Publish dateSep 2, 2020
AuthorsMatteo Allegretti / Christian E Zimmerli / Vasileios Rantos / Florian Wilfling / Paolo Ronchi / Herman K H Fung / Chia-Wei Lee / Wim Hagen / Beata Turoňová / Kai Karius / Mandy Börmel / Xiaojie Zhang / Christoph W Müller / Yannick Schwab / Julia Mahamid / Boris Pfander / Jan Kosinski / Martin Beck /
PubMed AbstractNuclear 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 ...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. 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 cells 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.
External linksNature / PubMed:32879490
MethodsEM (subtomogram averaging)
Resolution25.0 - 50.0 Å
Structure data

EMDB-10198:
In-cell S cerevisiae nuclear pore complex
Method: EM (subtomogram averaging) / Resolution: 25.0 Å

EMDB-10660:
Nup116_delta_NPC_25C
Method: EM (subtomogram averaging) / Resolution: 35.0 Å

EMDB-10661:
Nup116delta_NPC_37C
Method: EM (subtomogram averaging) / Resolution: 50.0 Å

Source
  • Saccharomyces cerevisiae (brewer's yeast)

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