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RAN MODULATES ALLOSTERIC CROSSTALK BETWEEN IMPORTIN β SURFACES.

Ying-Hui Ko1, Fenglin Li2, Stephanie Suinn1

  • 1Dept. of Biochemistry and Molecular Genetics, The University of Alabama at Birmingham, 1825 University Blvd, Birmingham, AL 35294, USA.

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Summary
This summary is machine-generated.

Ran-GTP regulates nuclear import by altering importin β structure, closing FG-binding pockets, and releasing cargo. This allosteric mechanism explains how nuclear transport is controlled.

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Area of Science:

  • Molecular Biology
  • Cell Biology
  • Structural Biology

Background:

  • Nuclear Pore Complex (NPC) facilitates transport between the nucleus and cytoplasm.
  • Ran GTPase gradient regulates nuclear import and export.
  • Importin β mediates cargo transport through the NPC.

Purpose of the Study:

  • To elucidate the structural mechanisms by which Ran-GTP modulates importin β activity.
  • To understand the conformational changes in importin β during nuclear import.

Main Methods:

  • Cryo-electron microscopy (cryo-EM) single particle analysis.
  • Biochemical activity assays.
  • Structural comparison of importin β in four distinct states.

Main Results:

  • Identified four distinct conformational states of importin β with different binding partners.
  • Demonstrated that Ran-GTP constrains importin β's structure, closing FG-binding pockets.
  • Revealed an allosteric mechanism involving crosstalk between importin β surfaces.

Conclusions:

  • Ran-GTP allosterically regulates importin β by closing FG-binding pockets, facilitating nuclear import.
  • This mechanism explains cargo release and NPC passage.
  • The proposed allosteric mechanism is likely conserved across β-karyopherins.