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Integrative structure and functional anatomy of a nuclear pore complex

Author

Listed:
  • Seung Joong Kim

    (University of California)

  • Javier Fernandez-Martinez

    (Laboratory of Cellular and Structural Biology, The Rockefeller University)

  • Ilona Nudelman

    (Laboratory of Cellular and Structural Biology, The Rockefeller University)

  • Yi Shi

    (Laboratory of Mass Spectrometry and Gaseous Ion Chemistry, The Rockefeller University
    University of Pittsburgh School of Medicine)

  • Wenzhu Zhang

    (Laboratory of Mass Spectrometry and Gaseous Ion Chemistry, The Rockefeller University)

  • Barak Raveh

    (University of California)

  • Thurston Herricks

    (Institute for Systems Biology)

  • Brian D. Slaughter

    (Stowers Institute for Medical Research)

  • Joanna A. Hogan

    (Indiana University, Bloomington)

  • Paula Upla

    (New York University School of Medicine)

  • Ilan E. Chemmama

    (University of California)

  • Riccardo Pellarin

    (University of California
    Institut Pasteur, CNRS UMR 3528)

  • Ignacia Echeverria

    (University of California)

  • Manjunatha Shivaraju

    (Stowers Institute for Medical Research)

  • Azraa S. Chaudhury

    (Laboratory of Cellular and Structural Biology, The Rockefeller University)

  • Junjie Wang

    (Laboratory of Mass Spectrometry and Gaseous Ion Chemistry, The Rockefeller University)

  • Rosemary Williams

    (Laboratory of Cellular and Structural Biology, The Rockefeller University)

  • Jay R. Unruh

    (Stowers Institute for Medical Research)

  • Charles H. Greenberg

    (University of California)

  • Erica Y. Jacobs

    (Laboratory of Mass Spectrometry and Gaseous Ion Chemistry, The Rockefeller University)

  • Zhiheng Yu

    (Janelia Research Campus, Howard Hughes Medical Institute)

  • M. Jason de la Cruz

    (Janelia Research Campus, Howard Hughes Medical Institute
    Structural Biology Program, Sloan Kettering Institute, Memorial Sloan Kettering Cancer Center)

  • Roxana Mironska

    (Laboratory of Cellular and Structural Biology, The Rockefeller University)

  • David L. Stokes

    (New York University School of Medicine)

  • John D. Aitchison

    (Institute for Systems Biology
    Center for Infectious Disease Research)

  • Martin F. Jarrold

    (Indiana University, Bloomington)

  • Jennifer L. Gerton

    (Stowers Institute for Medical Research)

  • Steven J. Ludtke

    (Baylor College of Medicine)

  • Christopher W. Akey

    (Boston University School of Medicine)

  • Brian T. Chait

    (Laboratory of Mass Spectrometry and Gaseous Ion Chemistry, The Rockefeller University)

  • Andrej Sali

    (University of California)

  • Michael P. Rout

    (Laboratory of Cellular and Structural Biology, The Rockefeller University)

Abstract

Nuclear pore complexes play central roles as gatekeepers of RNA and protein transport between the cytoplasm and nucleoplasm. However, their large size and dynamic nature have impeded a full structural and functional elucidation. Here we determined the structure of the entire 552-protein nuclear pore complex of the yeast Saccharomyces cerevisiae at sub-nanometre precision by satisfying a wide range of data relating to the molecular arrangement of its constituents. The nuclear pore complex incorporates sturdy diagonal columns and connector cables attached to these columns, imbuing the structure with strength and flexibility. These cables also tie together all other elements of the nuclear pore complex, including membrane-interacting regions, outer rings and RNA-processing platforms. Inwardly directed anchors create a high density of transport factor-docking Phe-Gly repeats in the central channel, organized into distinct functional units. This integrative structure enables us to rationalize the architecture, transport mechanism and evolutionary origins of the nuclear pore complex.

Suggested Citation

  • Seung Joong Kim & Javier Fernandez-Martinez & Ilona Nudelman & Yi Shi & Wenzhu Zhang & Barak Raveh & Thurston Herricks & Brian D. Slaughter & Joanna A. Hogan & Paula Upla & Ilan E. Chemmama & Riccardo, 2018. "Integrative structure and functional anatomy of a nuclear pore complex," Nature, Nature, vol. 555(7697), pages 475-482, March.
    • Handle: RePEc:nat:nature:v:555:y:2018:i:7697:d:10.1038_nature26003
    DOI: 10.1038/nature26003
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    Cited by:

    1. Maximilian Seidel & Anja Becker & Filipa Pereira & Jonathan J. M. Landry & Nayara Trevisan Doimo Azevedo & Claudia M. Fusco & Eva Kaindl & Natalie Romanov & Janina Baumbach & Julian D. Langer & Erin M, 2022. "Co-translational assembly orchestrates competing biogenesis pathways," Nature Communications, Nature, vol. 13(1), pages 1-15, December.
    2. Amanda M. Gleixner & Brandie Morris Verdone & Charlton G. Otte & Eric N. Anderson & Nandini Ramesh & Olivia R. Shapiro & Jenna R. Gale & Jocelyn C. Mauna & Jacob R. Mann & Katie E. Copley & Elizabeth , 2022. "NUP62 localizes to ALS/FTLD pathological assemblies and contributes to TDP-43 insolubility," Nature Communications, Nature, vol. 13(1), pages 1-17, December.
    3. David Winogradoff & Han-Yi Chou & Christopher Maffeo & Aleksei Aksimentiev, 2022. "Percolation transition prescribes protein size-specific barrier to passive transport through the nuclear pore complex," Nature Communications, Nature, vol. 13(1), pages 1-16, December.

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