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Related Experiment Videos

Ran alters nuclear pore complex conformation.

M W Goldberg1, S A Rutherford, M Hughes

  • 1CRC Department of Structural Cell Biology, Paterson Institute for Cancer Research, Christie Hospital, Wilmslow Road, Manchester, M20 9BX, UK. mgoldberg@picr.man.ac.uk

Journal of Molecular Biology
|July 8, 2000
PubMed
Summary
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Nuclear pore complex (NPC) transport involves Ran, a GTPase. RanGTP, not RanGDP, alters NPC structure and cytoplasmic filaments, suggesting Ran

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Nuclear pore complex (NPC) facilitates transport between the nucleus and cytoplasm.
  • Ran, a small GTPase, regulates nucleocytoplasmic transport, existing as GDP-bound (import) or GTP-bound (export) forms.
  • The dynamic NPC structure implies a potential active role in translocation.

Purpose of the Study:

  • To investigate the effect of RanGTP and RanGDP on NPC structure and function.
  • To determine if Ran actively modifies NPC conformation during transport.

Main Methods:

  • Injection of RanGTP and RanGDP into the cytoplasm of Xenopus oocytes.
  • Observation of NPC structural alterations using microscopy.
  • Tracking of nucleoplasmin-gold particle distribution.

Related Experiment Videos

Main Results:

  • RanGTP, but not RanGDP, induced NPC structural changes, including compaction and cytoplasmic filament extension.
  • RanGTP promoted nucleoplasmin-gold accumulation along extended cytoplasmic filaments.
  • RanGDP caused nucleoplasmin-gold accumulation at the NPC cytoplasmic rim.

Conclusions:

  • RanGTP plays a role in altering NPC cytoplasmic filament conformation.
  • This conformational change may be a mechanism by which Ran influences nucleocytoplasmic transport.