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The molecular architecture of the nuclear pore complex

Author

Listed:
  • 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,
    Present addresses: Laboratory of Nucleocytoplasmic Transport, Institut Jacques Monod, 2 place Jussieu, Tour 43, Paris 75251, France (S.D.); Department of Biochemistry, University of Groningen, Nijenborgh 4, 9747 AG Groningen, The Netherlands (L.M.V.); German Aerospace Center (PT-DLR), Heinrich-Konen-Strasse 1, D-53227 Bonn, Germany (J.K.); Structural Bioinformatics, EMBL, Meyerhofstrasse 1, D-69117 Heidelberg, Germany (D.D.); Office of Technology Transfer, The Rockefeller University, 1230 York Avenue, New York, New York 10065, USA (A.S.); Herbert Irving Comprehensive Cancer Centre, Columbia University, 1130 St Nicholas Avenue, New York, New York 10032, USA (O.K.-S.).)

  • Liesbeth M. Veenhoff

    (Laboratory of Cellular and Structural Biology, and,
    Present addresses: Laboratory of Nucleocytoplasmic Transport, Institut Jacques Monod, 2 place Jussieu, Tour 43, Paris 75251, France (S.D.); Department of Biochemistry, University of Groningen, Nijenborgh 4, 9747 AG Groningen, The Netherlands (L.M.V.); German Aerospace Center (PT-DLR), Heinrich-Konen-Strasse 1, D-53227 Bonn, Germany (J.K.); Structural Bioinformatics, EMBL, Meyerhofstrasse 1, D-69117 Heidelberg, Germany (D.D.); Office of Technology Transfer, The Rockefeller University, 1230 York Avenue, New York, New York 10065, USA (A.S.); Herbert Irving Comprehensive Cancer Centre, Columbia University, 1130 St Nicholas Avenue, New York, New York 10032, USA (O.K.-S.).)

  • 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,
    Present addresses: Laboratory of Nucleocytoplasmic Transport, Institut Jacques Monod, 2 place Jussieu, Tour 43, Paris 75251, France (S.D.); Department of Biochemistry, University of Groningen, Nijenborgh 4, 9747 AG Groningen, The Netherlands (L.M.V.); German Aerospace Center (PT-DLR), Heinrich-Konen-Strasse 1, D-53227 Bonn, Germany (J.K.); Structural Bioinformatics, EMBL, Meyerhofstrasse 1, D-69117 Heidelberg, Germany (D.D.); Office of Technology Transfer, The Rockefeller University, 1230 York Avenue, New York, New York 10065, USA (A.S.); Herbert Irving Comprehensive Cancer Centre, Columbia University, 1130 St Nicholas Avenue, New York, New York 10032, USA (O.K.-S.).)

  • 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
    Present addresses: Laboratory of Nucleocytoplasmic Transport, Institut Jacques Monod, 2 place Jussieu, Tour 43, Paris 75251, France (S.D.); Department of Biochemistry, University of Groningen, Nijenborgh 4, 9747 AG Groningen, The Netherlands (L.M.V.); German Aerospace Center (PT-DLR), Heinrich-Konen-Strasse 1, D-53227 Bonn, Germany (J.K.); Structural Bioinformatics, EMBL, Meyerhofstrasse 1, D-69117 Heidelberg, Germany (D.D.); Office of Technology Transfer, The Rockefeller University, 1230 York Avenue, New York, New York 10065, USA (A.S.); Herbert Irving Comprehensive Cancer Centre, Columbia University, 1130 St Nicholas Avenue, New York, New York 10032, USA (O.K.-S.).)

  • Adisetyantari Suprapto

    (Laboratory of Cellular and Structural Biology, and,
    Present addresses: Laboratory of Nucleocytoplasmic Transport, Institut Jacques Monod, 2 place Jussieu, Tour 43, Paris 75251, France (S.D.); Department of Biochemistry, University of Groningen, Nijenborgh 4, 9747 AG Groningen, The Netherlands (L.M.V.); German Aerospace Center (PT-DLR), Heinrich-Konen-Strasse 1, D-53227 Bonn, Germany (J.K.); Structural Bioinformatics, EMBL, Meyerhofstrasse 1, D-69117 Heidelberg, Germany (D.D.); Office of Technology Transfer, The Rockefeller University, 1230 York Avenue, New York, New York 10065, USA (A.S.); Herbert Irving Comprehensive Cancer Centre, Columbia University, 1130 St Nicholas Avenue, New York, New York 10032, USA (O.K.-S.).)

  • Orit Karni-Schmidt

    (Laboratory of Cellular and Structural Biology, and,
    Present addresses: Laboratory of Nucleocytoplasmic Transport, Institut Jacques Monod, 2 place Jussieu, Tour 43, Paris 75251, France (S.D.); Department of Biochemistry, University of Groningen, Nijenborgh 4, 9747 AG Groningen, The Netherlands (L.M.V.); German Aerospace Center (PT-DLR), Heinrich-Konen-Strasse 1, D-53227 Bonn, Germany (J.K.); Structural Bioinformatics, EMBL, Meyerhofstrasse 1, D-69117 Heidelberg, Germany (D.D.); Office of Technology Transfer, The Rockefeller University, 1230 York Avenue, New York, New York 10065, USA (A.S.); Herbert Irving Comprehensive Cancer Centre, Columbia University, 1130 St Nicholas Avenue, New York, New York 10032, USA (O.K.-S.).)

  • 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,)

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.

Suggested Citation

  • 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, 2007. "The molecular architecture of the nuclear pore complex," Nature, Nature, vol. 450(7170), pages 695-701, November.
    • Handle: RePEc:nat:nature:v:450:y:2007:i:7170:d:10.1038_nature06405
    DOI: 10.1038/nature06405
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    Cited by:

    1. Bálint Mészáros & István Simon & Zsuzsanna Dosztányi, 2009. "Prediction of Protein Binding Regions in Disordered Proteins," PLOS Computational Biology, Public Library of Science, vol. 5(5), pages 1-18, May.
    2. Daniel Russel & Keren Lasker & Ben Webb & Javier Velázquez-Muriel & Elina Tjioe & Dina Schneidman-Duhovny & Bret Peterson & Andrej Sali, 2012. "Putting the Pieces Together: Integrative Modeling Platform Software for Structure Determination of Macromolecular Assemblies," PLOS Biology, Public Library of Science, vol. 10(1), pages 1-5, January.
    3. V V Krishnan & Edmond Y Lau & Justin Yamada & Daniel P Denning & Samir S Patel & Michael E Colvin & Michael F Rexach, 2008. "Intramolecular Cohesion of Coils Mediated by Phenylalanine–Glycine Motifs in the Natively Unfolded Domain of a Nucleoporin," PLOS Computational Biology, Public Library of Science, vol. 4(8), pages 1-13, August.

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