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Ran modulates allosteric crosstalk between importin β surfaces.

Ying-Hui Ko1, Fenglin Li2, Stephanie S Suinn1

  • 1Department of Biochemistry and Molecular Genetics, The University of Alabama at Birmingham, Birmingham, AL, USA.

Nature Communications
|December 11, 2025
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Summary
This summary is machine-generated.

Ran-GTP regulates nuclear import by altering importin β structure. This mechanism, revealed by cryo-EM, explains how cargo is released into the nucleus, impacting nuclear transport.

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Area of Science:

  • Molecular Biology
  • Structural Biology
  • Cell Biology

Background:

  • Nuclear transport relies on the GTPase Ran gradient and importin β.
  • Ran-GTP's precise role in modulating importin β activity during nuclear import is not fully understood.
  • Importin β interacts with phenylalanine-glycine-rich nucleoporins (FG-nups) to facilitate cargo passage.

Purpose of the Study:

  • To elucidate the structural mechanisms by which Ran-GTP modulates importin β activity.
  • To characterize the conformational states of importin β in complex with key import/export factors.
  • To correlate structural findings with biochemical data to understand nuclear import regulation.

Main Methods:

  • Cryogenic electron microscopy (cryo-EM) single-particle analysis was used to determine structures.
  • Five distinct conformational states of importin β with various effectors were resolved.
  • Biochemical assays were performed to correlate structural data with functional activities.

Main Results:

  • Ran-GTP, but not Ran-GDP, induces a constrained solenoid structure in importin β.
  • This structural change closes high-affinity FG-binding pockets on importin β.
  • Ran-GTP allosterically displaces import cargo by altering interactions between importin β surfaces.

Conclusions:

  • Ran-GTP binding induces conformational changes in importin β, regulating its interaction with FG-nups and cargo release.
  • An allosteric mechanism explains how Ran-GTP facilitates nuclear import and cargo dissociation.
  • This proposed allosteric mechanism is likely applicable to other β-karyopherins involved in nuclear transport.