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Structure. 2017 Feb 2. pii: S0969-2126(17)30006-0. doi: 10.1016/j.str.2017.01.006. [Epub ahead of print]

Molecular Architecture of the Major Membrane Ring Component of the Nuclear Pore Complex.

Author information

  • 1Skirball Institute and Department of Cell Biology, New York University School of Medicine, New York, NY 10016, USA; Laboratory of Cellular and Structural Biology, The Rockefeller University, Box 213, 1230 York Avenue, New York, NY 10065, USA.
  • 2Department of Bioengineering and Therapeutic Sciences, Department of Pharmaceutical Chemistry, California Institute for Quantitative Biosciences, UCSF MC 2552, Byers Hall at Mission Bay, 1700 4th Street, Suite 503B, University of California, San Francisco, San Francisco, CA 94158, USA.
  • 3Department of Biochemistry, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, NY 10461, USA.
  • 4New York Structural Biology Center, New York, NY 10027, USA.
  • 5Laboratory of Cellular and Structural Biology, The Rockefeller University, Box 213, 1230 York Avenue, New York, NY 10065, USA.
  • 6Simons Electron Microscopy Center at New York Structural Biology Center, New York, NY 10027, USA.
  • 7Skirball Institute and Department of Cell Biology, New York University School of Medicine, New York, NY 10016, USA.
  • 8Department of Bioengineering and Therapeutic Sciences, Department of Pharmaceutical Chemistry, California Institute for Quantitative Biosciences, UCSF MC 2552, Byers Hall at Mission Bay, 1700 4th Street, Suite 503B, University of California, San Francisco, San Francisco, CA 94158, USA. Electronic address: sali@salilab.org.
  • 9Laboratory of Cellular and Structural Biology, The Rockefeller University, Box 213, 1230 York Avenue, New York, NY 10065, USA. Electronic address: rout@rockefeller.edu.
  • 10Laboratory of Cellular and Structural Biology, The Rockefeller University, Box 213, 1230 York Avenue, New York, NY 10065, USA. Electronic address: jfernandez@rockefeller.edu.

Abstract

The membrane ring that equatorially circumscribes the nuclear pore complex (NPC) in the perinuclear lumen of the nuclear envelope is composed largely of Pom152 in yeast and its ortholog Nup210 (or Gp210) in vertebrates. Here, we have used a combination of negative-stain electron microscopy, nuclear magnetic resonance, and small-angle X-ray scattering methods to determine an integrative structure of the ∼120 kDa luminal domain of Pom152. Our structural analysis reveals that the luminal domain is formed by a flexible string-of-pearls arrangement of nine repetitive cadherin-like Ig-like domains, indicating an evolutionary connection between NPCs and the cell adhesion machinery. The 16 copies of Pom152 known to be present in the yeast NPC are long enough to form the observed membrane ring, suggesting how interactions between Pom152 molecules help establish and maintain the NPC architecture.

KEYWORDS:

Gp210; NMR; Nup210; Pom152; SAXS; cadherin; electron microscopy; integrative structure determination; nuclear pore complex; nucleoporin

PMID:
28162953
DOI:
10.1016/j.str.2017.01.006
[PubMed - as supplied by publisher]
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