The molecular architecture of the nuclear pore complex

Frank Alber, Svetlana Dokudovskaya, Liesbeth M. Veenhoff, Wenzhu Zhang, Julia Kipper, Damien Devos, Adisetyantari Suprapto, Orit Karni-Schmidt, Rosemary Williams, Brian T. Chait (), Andrej Sali () and Michael P. Rout ()
Additional contact information
Frank Alber: and California Institute for Quantitative Biosciences, Mission Bay QB3, 1700 4th Street, Suite 503B, University of California at San Francisco, San Francisco, California 94158-2330, USA
Svetlana Dokudovskaya: Laboratory of Cellular and Structural Biology, and,
Liesbeth M. Veenhoff: Laboratory of Cellular and Structural Biology, and,
Wenzhu Zhang: Laboratory of Mass Spectrometry and Gaseous Ion Chemistry, The Rockefeller University, 1230 York Avenue, New York, New York 10065, USA
Julia Kipper: Laboratory of Cellular and Structural Biology, and,
Damien Devos: and California Institute for Quantitative Biosciences, Mission Bay QB3, 1700 4th Street, Suite 503B, University of California at San Francisco, San Francisco, California 94158-2330, USA
Adisetyantari Suprapto: Laboratory of Cellular and Structural Biology, and,
Orit Karni-Schmidt: Laboratory of Cellular and Structural Biology, and,
Rosemary Williams: Laboratory of Cellular and Structural Biology, and,
Brian T. Chait: Laboratory of Mass Spectrometry and Gaseous Ion Chemistry, The Rockefeller University, 1230 York Avenue, New York, New York 10065, USA
Andrej Sali: and California Institute for Quantitative Biosciences, Mission Bay QB3, 1700 4th Street, Suite 503B, University of California at San Francisco, San Francisco, California 94158-2330, USA
Michael P. Rout: Laboratory of Cellular and Structural Biology, and,

Nature, 2007, vol. 450, issue 7170, 695-701

Abstract: Abstract Nuclear pore complexes (NPCs) are proteinaceous assemblies of approximately 50 MDa that selectively transport cargoes across the nuclear envelope. To determine the molecular architecture of the yeast NPC, we collected a diverse set of biophysical and proteomic data, and developed a method for using these data to localize the NPC’s 456 constituent proteins (see the accompanying paper). Our structure reveals that half of the NPC is made up of a core scaffold, which is structurally analogous to vesicle-coating complexes. This scaffold forms an interlaced network that coats the entire curved surface of the nuclear envelope membrane within which the NPC is embedded. The selective barrier for transport is formed by large numbers of proteins with disordered regions that line the inner face of the scaffold. The NPC consists of only a few structural modules that resemble each other in terms of the configuration of their homologous constituents, the most striking of these being a 16-fold repetition of ‘columns’. These findings provide clues to the evolutionary origins of the NPC.

Date: 2007
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DOI: 10.1038/nature06405

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