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The nucleus restricts several proteins within and allows others to pass. The restricted proteins possess a nuclear retention sequence or NRS, anchoring them to the nuclear lamins and preventing their transport to the cytosol. The non-restricted proteins, after their synthesis, are transported to their site of action, such as the cytosol or other organelles, with the help of nuclear export signals or NES.
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Structural Basis for Selective Binding of Export Cargoes by Exportin-5.

Ryuji Yamazawa1, Chimari Jiko2, Saehae Choi3

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Structure (London, England : 1993)
|August 14, 2018
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Summary

Exportin-5 (Exp-5) undergoes a conformational change upon binding RanGTP, creating a selective cage for cargo like pre-miRNA. This structural insight clarifies the molecular mechanism of nuclear export.

Keywords:
RanGTPcargo selection mechanismexportin 5heat repeatspre-microRNA

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Area of Science:

  • Molecular Biology
  • Structural Biology
  • Biochemistry

Background:

  • Nuclear transport relies on proteins like importins and exportins interacting with RanGTP.
  • Exportins facilitate the movement of specific cargo from the nucleus to the cytoplasm.
  • Understanding exportin conformational changes is key to deciphering nuclear export regulation.

Purpose of the Study:

  • To elucidate the structural basis of Exportin-5 (Exp-5) function.
  • To investigate the conformational changes of Exp-5 upon binding RanGTP.
  • To characterize the formation of the Exp-5:RanGTP complex and its implications for cargo binding.

Main Methods:

  • X-ray crystallography was used to determine the structures of Exp-5 alone and in complex with RanGTP.
  • Analysis of protein conformations and intermolecular interactions was performed.

Main Results:

  • The crystal structure of Exp-5 revealed a closed, ring-shaped conformation stabilized by intramolecular interactions.
  • RanGTP binding to Exp-5 disrupts these interactions, leading to a conformational rearrangement.
  • This rearrangement creates an open state in Exp-5, forming a selective binding site for RanGTP and subsequent cargo, such as pre-miRNA.

Conclusions:

  • Exportin-5 undergoes a significant conformational change upon RanGTP binding, transitioning from a closed to an open state.
  • This conformational flexibility is crucial for RanGTP-mediated cargo selection and nuclear export.
  • The study provides a structural framework for understanding how Exportin-5 functions as a selective transporter in the nucleus.