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Published March 2010 | Published
Journal Article Open

Characterization of the membrane-coating Nup84 complex: Paradigm for the nuclear pore complex structure


Nuclear pore complexes (NPCs) function as selective gates for nucleocytoplasmic transport. Although the NPC was discovered more than half a century ago, our knowledge of NPC components in atomic detail has exploded only over the past few years. Recent structural, biochemical, and in vivo studies of NPC components, in particular the membrane-coating heptameric Nup84 complex, have shed light onto the NPC architecture as well as onto its dynamic nature. Striking similarities were revealed between the components of the NPC and of coat protein complexes in the endocytic and secretory pathways, supporting their common evolutionary origin in a progenitor protocoatomer. Here, we summarize these findings and discuss emerging concepts that underlie the molecular architecture and the dynamics of the NPC. We conclude that the uncovered principles are not limited to the NPC, but are likely to extend to other macromolecular assemblies.

Additional Information

© 2010 Landes Bioscience. Submitted: 01/03/10; Accepted: 01/03/10. We thank Oliver Dreesen, Marc Elsliger, Thomas Huber, Stephan Kutik, Johanna Napetschnig, Alina Patke, Pete Stavropoulos, Till Strowig and Deniz Top for comments on the manuscript, Stephanie Etherton for help with editing of the manuscript, and Gunter Blobel for continuing support and advice. E.W.D. is the Dale F. and Betty Ann Frey Fellow of the Damon Runyon Cancer Research Foundation, DRG-1977-08, and A.H. is supported by a grant from the Leukemia and Lymphoma Society.

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