
Open access
Datum
2022-05-01Typ
- Review Article
Abstract
Nuclear pore complexes (NPCs) are the only transport channels that cross the nuclear envelope. Constructed from ~500–1000 nucleoporin proteins each, they are among the largest macromolecular assemblies in eukaryotic cells. Thanks to advances in structural analysis approaches, the construction principles and architecture of the NPC have recently been revealed at submolecular resolution. Although the overall structure and inventory of nucleoporins are conserved, NPCs exhibit significant compositional and functional plasticity even within single cells and surprising variability in their assembly pathways. Once assembled, NPCs remain seemingly unexchangeable in post-mitotic cells. There are a number of as yet unresolved questions about how the versatility of NPC assembly and composition is established, how cells monitor the functional state of NPCs or how they could be renewed. Here, we review current progress in our understanding of the key aspects of NPC architecture and lifecycle. Mehr anzeigen
Persistenter Link
https://doi.org/10.3929/ethz-b-000544953Publikationsstatus
publishedExterne Links
Zeitschrift / Serie
CellsBand
Seiten / Artikelnummer
Verlag
MDPIThema
nuclear pore complex; nucleoporin; NPC; membrane fusion; Ran; lipids; assembly factor; amphipathic helix; nuclear transport receptor; FG repeats; Brl1; autophagy; ageing; aggregation; neurodegneration