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Cell. 2016 Nov 17;167(5):1215-1228.e25. doi: 10.1016/j.cell.2016.10.028. Epub 2016 Nov 10.

Structure and Function of the Nuclear Pore Complex Cytoplasmic mRNA Export Platform.

Author information

  • 1Laboratory of Cellular and Structural Biology, The Rockefeller University, New York, NY 10065, USA.
  • 2Departments of Bioengineering and Therapeutic Sciences and Pharmaceutical Chemistry, California Institute for Quantitative Biosciences, University of California, San Francisco, San Francisco, CA 94158, USA.
  • 3Laboratory of Mass Spectrometry and Gaseous Ion Chemistry, The Rockefeller University, New York, NY 10065, USA.
  • 4Skirball Institute of Biomolecular Medicine, Department of Cell Biology, New York University School of Medicine, New York, NY 10016, USA.
  • 5Departments of Bioengineering and Therapeutic Sciences and Pharmaceutical Chemistry, California Institute for Quantitative Biosciences, University of California, San Francisco, San Francisco, CA 94158, USA; Structural Bioinformatics Unit, Institut Pasteur, CNRS UMR 3528, 75015 Paris, France.
  • 6Département de Biochimie et Médecine Moléculaire, University of Montréal, Montréal, QC H3C3J7, Canada.
  • 7Simons Electron Microscopy Center at New York Structural Biology Center, New York, NY 10027, USA.
  • 8Laboratory of Mass Spectrometry and Gaseous Ion Chemistry, The Rockefeller University, New York, NY 10065, USA. Electronic address: chait@rockefeller.edu.
  • 9Departments of Bioengineering and Therapeutic Sciences and Pharmaceutical Chemistry, California Institute for Quantitative Biosciences, University of California, San Francisco, San Francisco, CA 94158, USA. Electronic address: sali@salilab.org.
  • 10Laboratory of Cellular and Structural Biology, The Rockefeller University, New York, NY 10065, USA. Electronic address: rout@rockefeller.edu.

Abstract

The last steps in mRNA export and remodeling are performed by the Nup82 complex, a large conserved assembly at the cytoplasmic face of the nuclear pore complex (NPC). By integrating diverse structural data, we have determined the molecular architecture of the native Nup82 complex at subnanometer precision. The complex consists of two compositionally identical multiprotein subunits that adopt different configurations. The Nup82 complex fits into the NPC through the outer ring Nup84 complex. Our map shows that this entire 14-MDa Nup82-Nup84 complex assembly positions the cytoplasmic mRNA export factor docking sites and messenger ribonucleoprotein (mRNP) remodeling machinery right over the NPC's central channel rather than on distal cytoplasmic filaments, as previously supposed. We suggest that this configuration efficiently captures and remodels exporting mRNP particles immediately upon reaching the cytoplasmic side of the NPC.

KEYWORDS:

Nup4 complex; Nup82 complex; computational structural biology; cross-linking and mass spectrometry; electron microscopy; integrative structure determination; mRNA export; mRNP remodeling; nuclear pore complex; small-angle X-ray scattering

PMID:
27839866
PMCID:
PMC5130164
[Available on 2017-11-17]
DOI:
10.1016/j.cell.2016.10.028
[PubMed - in process]
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