| Literature DB >> 30943044 |
Bernhard Hampoelz1, Amparo Andres-Pons1,2, Panagiotis Kastritis1,3, Martin Beck1,4,5.
Abstract
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.Keywords: NPC; NPC architecture; NPC assembly; nuclear pore complex; nuclear transport; nucleoporin
Year: 2019 PMID: 30943044 DOI: 10.1146/annurev-biophys-052118-115308
Source DB: PubMed Journal: Annu Rev Biophys ISSN: 1936-122X Impact factor: 12.981