Journal article
Structure and Assembly of the Nuclear Pore Complex
- Hampoelz, Bernhard Structural and Computational Biology Unit, European Molecular Biology Laboratory, 69117 Heidelberg, Germany;, ,
- Andres-Pons, Amparo Current affiliation: Friedrich Miescher Institute for Biomedical Research, 4058 Basel, Switzerland;
- Kastritis, Panagiotis Current affiliation: ZIK HALOmem, Martin Luther University of Halle-Wittenberg, 06120 Halle (Saale), Germany
- Beck, Martin Max Planck Institute of Biophysics, 60438 Frankfurt am Main, Germany
Published in:
- Annual Review of Biophysics. - Annual Reviews. - 2019, vol. 48, no. 1, p. 515-536
English
Nuclear pore complexes (NPCs) mediate nucleocytoplasmic exchange. They are exceptionally large protein complexes that fuse the inner and outer nuclear membranes to form channels across the nuclear envelope. About 30 different protein components, termed nucleoporins, assemble in multiple copies into an intricate cylindrical architecture. Here, we review our current knowledge of the structure of nucleoporins and how those come together in situ. We delineate architectural principles on several hierarchical organization levels, including isoforms, posttranslational modifications, nucleoporins, and higher-order oligomerization of nucleoporin subcomplexes. We discuss how cells exploit this modularity to faithfully assemble NPCs.
- Language
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- English
- Open access status
- closed
- Identifiers
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- DOI 10.1146/annurev-biophys-052118-115308
- ISSN 1936-122X
- Persistent URL
- https://sonar.ch/global/documents/63983
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