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Integrative structure and functional anatomy of a nuclear pore complex.
Kim, Seung Joong; Fernandez-Martinez, Javier; Nudelman, Ilona; Shi, Yi; Zhang, Wenzhu; Raveh, Barak; Herricks, Thurston; Slaughter, Brian D; Hogan, Joanna A; Upla, Paula; Chemmama, Ilan E; Pellarin, Riccardo; Echeverria, Ignacia; Shivaraju, Manjunatha; Chaudhury, Azraa S; Wang, Junjie; Williams, Rosemary; Unruh, Jay R; Greenberg, Charles H; Jacobs, Erica Y; Yu, Zhiheng; de la Cruz, M Jason; Mironska, Roxana; Stokes, David L; Aitchison, John D; Jarrold, Martin F; Gerton, Jennifer L; Ludtke, Steven J; Akey, Christopher W; Chait, Brian T; Sali, Andrej; Rout, Michael P.
Afiliação
  • Kim SJ; Department of Bioengineering and Therapeutic Sciences, Department of Pharmaceutical Chemistry, and California Institute for Quantitative Biosciences, University of California, San Francisco, San Francisco, California 94158, USA.
  • Fernandez-Martinez J; Laboratory of Cellular and Structural Biology, The Rockefeller University, New York, New York 10065, USA.
  • Nudelman I; Laboratory of Cellular and Structural Biology, The Rockefeller University, New York, New York 10065, USA.
  • Shi Y; Laboratory of Mass Spectrometry and Gaseous Ion Chemistry, The Rockefeller University, New York, New York 10065, USA.
  • Zhang W; Laboratory of Mass Spectrometry and Gaseous Ion Chemistry, The Rockefeller University, New York, New York 10065, USA.
  • Raveh B; Department of Bioengineering and Therapeutic Sciences, Department of Pharmaceutical Chemistry, and California Institute for Quantitative Biosciences, University of California, San Francisco, San Francisco, California 94158, USA.
  • Herricks T; Institute for Systems Biology, 401 Terry Ave. N., Seattle, Washington 98109, USA.
  • Slaughter BD; Stowers Institute for Medical Research, Kansas City, Missouri 64110, USA.
  • Hogan JA; Department of Chemistry, Indiana University, Bloomington, Indiana 47405, USA.
  • Upla P; Skirball Institute and Department of Cell Biology, New York University School of Medicine, New York, New York 10016, USA.
  • Chemmama IE; Department of Bioengineering and Therapeutic Sciences, Department of Pharmaceutical Chemistry, and California Institute for Quantitative Biosciences, University of California, San Francisco, San Francisco, California 94158, USA.
  • Pellarin R; Department of Bioengineering and Therapeutic Sciences, Department of Pharmaceutical Chemistry, and California Institute for Quantitative Biosciences, University of California, San Francisco, San Francisco, California 94158, USA.
  • Echeverria I; Department of Bioengineering and Therapeutic Sciences, Department of Pharmaceutical Chemistry, and California Institute for Quantitative Biosciences, University of California, San Francisco, San Francisco, California 94158, USA.
  • Shivaraju M; Stowers Institute for Medical Research, Kansas City, Missouri 64110, USA.
  • Chaudhury AS; Laboratory of Cellular and Structural Biology, The Rockefeller University, New York, New York 10065, USA.
  • Wang J; Laboratory of Mass Spectrometry and Gaseous Ion Chemistry, The Rockefeller University, New York, New York 10065, USA.
  • Williams R; Laboratory of Cellular and Structural Biology, The Rockefeller University, New York, New York 10065, USA.
  • Unruh JR; Stowers Institute for Medical Research, Kansas City, Missouri 64110, USA.
  • Greenberg CH; Department of Bioengineering and Therapeutic Sciences, Department of Pharmaceutical Chemistry, and California Institute for Quantitative Biosciences, University of California, San Francisco, San Francisco, California 94158, USA.
  • Jacobs EY; Laboratory of Mass Spectrometry and Gaseous Ion Chemistry, The Rockefeller University, New York, New York 10065, USA.
  • Yu Z; Janelia Research Campus, Howard Hughes Medical Institute, 19700 Helix Drive, Ashburn, Virginia 20148, USA.
  • de la Cruz MJ; Janelia Research Campus, Howard Hughes Medical Institute, 19700 Helix Drive, Ashburn, Virginia 20148, USA.
  • Mironska R; Laboratory of Cellular and Structural Biology, The Rockefeller University, New York, New York 10065, USA.
  • Stokes DL; Skirball Institute and Department of Cell Biology, New York University School of Medicine, New York, New York 10016, USA.
  • Aitchison JD; Institute for Systems Biology, 401 Terry Ave. N., Seattle, Washington 98109, USA.
  • Jarrold MF; Center for Infectious Disease Research, Seattle, Washington 98109, USA.
  • Gerton JL; Department of Chemistry, Indiana University, Bloomington, Indiana 47405, USA.
  • Ludtke SJ; Stowers Institute for Medical Research, Kansas City, Missouri 64110, USA.
  • Akey CW; Verna and Marrs McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine, 1 Baylor Plaza, Houston, Texas 77030, USA.
  • Chait BT; Department of Physiology and Biophysics, Boston University School of Medicine, 700 Albany Street, Boston, Massachusetts 02118, USA.
  • Sali A; Laboratory of Mass Spectrometry and Gaseous Ion Chemistry, The Rockefeller University, New York, New York 10065, USA.
  • Rout MP; Department of Bioengineering and Therapeutic Sciences, Department of Pharmaceutical Chemistry, and California Institute for Quantitative Biosciences, University of California, San Francisco, San Francisco, California 94158, USA.
Nature ; 555(7697): 475-482, 2018 03 22.
Article em En | MEDLINE | ID: mdl-29539637
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.
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Texto completo: 1 Base de dados: MEDLINE Assunto principal: Saccharomyces cerevisiae / Poro Nuclear / Complexo de Proteínas Formadoras de Poros Nucleares Tipo de estudo: Prognostic_studies Idioma: En Ano de publicação: 2018 Tipo de documento: Article
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Texto completo: 1 Base de dados: MEDLINE Assunto principal: Saccharomyces cerevisiae / Poro Nuclear / Complexo de Proteínas Formadoras de Poros Nucleares Tipo de estudo: Prognostic_studies Idioma: En Ano de publicação: 2018 Tipo de documento: Article