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Related Experiment Videos

Minimal nuclear pore complexes define FG repeat domains essential for transport.

Lisa A Strawn1, Tianxiang Shen, Nataliya Shulga

  • 1Department of Cell and Developmental Biology, Vanderbilt University Medical Center, 3120A MRBIII, 465 21st Avenue South, Nashville, TN 37232-8240, USA.

Nature Cell Biology
|March 25, 2004
PubMed
Summary

Researchers explored nuclear pore complex (NPC) protein interactions by deleting phenylalanine-glycine (FG) domains in yeast. Specific symmetric FG-Nup deletions were essential, revealing multiple NPC translocation pathways.

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Nuclear pore complexes (NPCs) regulate transport between the nucleus and cytoplasm.
  • Translocation relies on interactions between receptor-cargo complexes and phenylalanine-glycine (FG) repeats within FG-Nups.

Purpose of the Study:

  • To investigate the essentiality and function of FG domains in Saccharomyces cerevisiae FG-Nups.
  • To determine the impact of FG domain deletions on NPC structure and transport.

Main Methods:

  • Systematic deletion of FG domains from 11 Saccharomyces cerevisiae FG-Nups in various combinations.
  • Assessing viability, NPC permeability barrier, and import rates of specific karyopherins (Kap).

Main Results:

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  • Deletion of all five asymmetrically localized FG domains was non-essential.
  • Specific combinations of symmetrically localized FG domains were found to be essential.
  • Over 50% of FG domain mass could be deleted without affecting viability or the NPC permeability barrier.
  • Symmetric deletions mildly reduced Kap95-Kap60 import but abolished Kap104 import.

    • Conclusions:

    • The results suggest that NPC translocation is mediated by multiple pathways.
    • Symmetric FG-Nup domains play critical, distinct roles in nucleocytoplasmic transport.