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Updated: Sep 10, 2025

Detection of Small GTPase Prenylation and GTP Binding Using Membrane Fractionation and GTPase-linked Immunosorbent Assay
Published on: November 11, 2018
The small GTPase Ran defines nuclear pore complex asymmetry
Jenny Sachweh1, Mandy Börmel2, Sven Klumpe3
1Department of Molecular Sociology, Max Planck Institute of Biophysics, Frankfurt am Main, Germany.
Nuclear pore complexes (NPCs) are key to nucleocytoplasmic exchange. This study reveals how NPCs achieve asymmetric structure from a symmetric scaffold, controlled by the Ran GTPase, suggesting a self-regulatory transport system.
Area of Science:
- Cell Biology
- Structural Biology
- Molecular Biology
Background:
- Nuclear pore complexes (NPCs) regulate transport between the nucleus and cytoplasm.
- NPCs exhibit asymmetric structures crucial for directional transport.
- The assembly of these asymmetric structures onto a symmetric scaffold remained poorly understood.
Purpose of the Study:
- To elucidate the mechanism of asymmetric nuclear pore complex assembly.
- To investigate the role of the Ran GTPase in NPC structure and function.
- To understand the self-regulatory nature of the nuclear transport system.
Main Methods:
- Cryo-electron tomography
- Subtomogram averaging
- Template matching
- Live imaging in budding yeast and Drosophila
- Genetic induction of ectopic nuclear pores
Main Results:
- Ectopic nuclear pores formed outside the nuclear envelope were found to be symmetric.
- The peripheral structure of NPCs is influenced by the nucleotide state of the Ran GTPase.
- Evidence suggests a unified mechanism controls both NPC transport and composition.
Conclusions:
- The nuclear transport system is self-regulatory.
- The same molecular mechanism governs both nucleocytoplasmic transport and the composition of the transport channel.
- Ran GTPase plays a critical role in establishing NPC asymmetry.
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