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Related Experiment Video

Updated: May 4, 2026

The MultiBac Protein Complex Production Platform at the EMBL
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Structural basis for the assembly of a nuclear export complex.

Yoshiyuki Matsuura1, Murray Stewart

  • 1MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, UK.

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|December 17, 2004
PubMed
Summary

This study reveals the crystal structure of a nuclear export complex, detailing how exportins bind cargo and RanGTP to facilitate nuclear protein export. This provides a molecular basis for understanding nuclear transport regulation.

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Area of Science:

  • Molecular Biology
  • Structural Biology
  • Cell Biology

Background:

  • Nuclear pore complexes regulate macromolecular transport between the nucleus and cytoplasm.
  • Importins and exportins are key transport carriers, with RanGTP orchestrating directionality.
  • RanGTP dissociates cargo from importins but is required for exportin-cargo binding.

Purpose of the Study:

  • To elucidate the structural basis of nuclear protein export.
  • To provide a framework for understanding the distinct roles of RanGTP in import and export.
  • To characterize the export complex formed by exportin Cse1p, Kap60p, and RanGTP.

Main Methods:

  • X-ray crystallography (2.0 Å resolution)
  • Structural analysis of the ternary export complex
  • Site-directed mutagenesis

Main Results:

  • The crystal structure reveals exportin Cse1p coiling around RanGTP and Kap60p.
  • Cse1p stabilizes the RanGTP-bound state and clamps the importin-beta-binding domain of Kap60p.
  • Mutagenesis shows conformational changes couple cargo binding to RanGTP affinity, facilitating complex disassembly.

Conclusions:

  • The structure provides a molecular mechanism for nuclear export mediated by exportin Cse1p.
  • Exportin conformational changes are critical for coupling cargo binding and RanGTP interaction.
  • This mechanism ensures efficient and regulated export of cargo-free importins.