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A self-inhibitory interaction within Nup155 and membrane binding are required for nuclear pore complex formation
Paola De Magistris1,2, Marianna Tatarek-Nossol2, Manfred Dewor2
1Friedrich Miescher Laboratory of the Max Planck Society, Spemannstraße 39, 72076 Tübingen, Germany.
Journal of Cell Science
|November 19, 2017
Summary
Nuclear pore complexes (NPCs) form vital gateways. Nup93 binding to Nup53 is key for inner ring assembly, enabling NPC formation and nuclear envelope integration.
Area of Science:
- Cell Biology
- Molecular Biology
- Structural Biology
Background:
- Nuclear pore complexes (NPCs) regulate transport between the nucleus and cytoplasm.
- NPCs possess a complex structure with distinct rings, crucial for their function.
- The assembly mechanism of the NPC inner ring remains incompletely understood.
Purpose of the Study:
- To investigate the role of Nup155 in the assembly of the NPC inner ring.
- To elucidate the regulatory mechanisms governing NPC formation.
- To understand how different nucleoporins interact during NPC biogenesis.
Main Methods:
- In vitro nuclear assembly reactions were utilized.
- Mutational analysis of Nup155 was performed, focusing on its N-terminal domain.
- Protein interaction studies were conducted to assess binding affinities.
Main Results:
- Direct pore membrane binding of Nup155 is essential for NPC assembly.
- A truncated Nup155 mutant could assemble outer ring components but blocked further inner ring progression.
- Nup155 self-interaction auto-inhibits its binding to Nup53.
- Nup93 binding to Nup53 overcomes this inhibition, facilitating inner ring formation.
Conclusions:
- Nup155's membrane binding is critical for initiating NPC assembly.
- Nup93 acts as a crucial mediator in Nup155-Nup53 interactions, driving inner ring formation.
- Understanding these interactions provides insights into the coordinated assembly of large protein complexes like NPCs.
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