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Journal Article

Structure and Assembly of the Nuclear Pore Complex

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Beck,  Martin       
Structural and Computational Biology Unit, European Molecular Biology Laboratory, Heidelberg, Germany;
Cell Biology and Biophysics Unit, European Molecular Biology Laboratory, Heidelberg, Germany;
Department of Molecular Sociology, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

Hampoelz, B., Andres-Pons, A., Kastritis, P., & Beck, M. (2019). Structure and Assembly of the Nuclear Pore Complex. Annual Review of Biophysics, 48, 515-536. doi:10.1146/annurev-biophys-052118-115308.


Cite as: https://hdl.handle.net/21.11116/0000-0003-527B-7
Abstract
Nuclear pore complexes (NPCs) mediate nucleocytoplasmic exchange.They are exceptionally large protein complexes that fuse the inner andouter nuclear membranes to form channels across the nuclear envelope.About 30 different protein components, termed nucleoporins, assemble inmultiple copies into an intricate cylindrical architecture. Here, we reviewour current knowledge of the structure of nucleoporins and how those cometogether in situ. We delineate architectural principles on several hierarchicalorganization levels, including isoforms, posttranslational modifications, nu-cleoporins, and higher-order oligomerization of nucleoporin subcomplexes.We discuss how cells exploit this modularity to faithfully assemble NPC.