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Atomic force microscopy reveals structural variability amongst nuclear pore complexes.

George J Stanley1, Ariberto Fassati2, Bart W Hoogenboom1,3

  • 1London Centre for Nanotechnology, University College London, London, UK.

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|November 21, 2018
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Summary
This summary is machine-generated.

High-resolution imaging reveals the dynamic structure of the nuclear pore complex (NPC) and its FG-Nup proteins. This structural diversity explains how NPCs facilitate nuclear transport, with importin-β showing strong binding.

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Area of Science:

  • Cell Biology
  • Structural Biology
  • Biophysics

Background:

  • The nuclear pore complex (NPC) regulates transport between the nucleus and cytoplasm.
  • NPC function relies on intrinsically disordered FG-Nup proteins within the central channel, whose structure remains poorly understood.
  • Previous studies have focused on NPC scaffold structure, leaving FG-Nup dynamics and nanomechanics uncharacterized.

Purpose of the Study:

  • To structurally and nanomechanically analyze individual nuclear pore complexes (NPCs).
  • To investigate the role of FG-Nup cohesiveness in NPC transport functionality.
  • To characterize the interactions between nuclear transport receptors and FG-Nups.

Main Methods:

  • High-resolution atomic force microscopy (AFM) was employed for structural and nanomechanical analysis.
  • AFM was used to study individual NPCs, revealing dynamic behaviors and pore size variations.
  • Interactions between different nuclear transport receptors and FG-Nups were examined.

Main Results:

  • AFM revealed structural diversity and dynamic behavior of NPC scaffolds and central channels.
  • NPCs exhibit varying pore sizes, suggesting a range of FG-Nup cohesiveness facilitating collective rearrangements.
  • Nuclear transport receptors interact differently with FG-Nups, with importin-β demonstrating particularly strong binding.

Conclusions:

  • The structural diversity of NPCs and their FG-Nup assemblies is crucial for regulating macromolecular transport.
  • FG-Nup cohesiveness allows for dynamic rearrangements, supporting the notion of facile nuclear transport.
  • Differential binding affinities of transport receptors, like importin-β, highlight the specificity of nuclear import pathways.