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The human homologue of yeast CRM1 is in a dynamic subcomplex with CAN/Nup214 and a novel nuclear pore component Nup88

M Fornerod1, J van Deursen, S van Baal

  • 1Department of Genetics, St Jude Children's Research Hospital, Memphis, TN 38105, USA.

The EMBO Journal
|February 17, 1997
PubMed

Insights

The oncogenic nucleoporin CAN/Nup214 is crucial for nuclear pore complex (NPC) function. Its interaction with Nup88 and human CRM1 (hCRM1) is vital for nuclear transport and cell viability.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Genetics

Background:

  • The oncogenic nucleoporin CAN/Nup214 plays a critical role in vertebrate cell function.
  • CAN/Nup214 depletion leads to nuclear protein import defects, mRNA export inhibition, and cell cycle arrest.

Purpose of the Study:

  • To identify and characterize proteins associated with CAN/Nup214.
  • To elucidate the functional relationship between CAN/Nup214, Nup88, and human CRM1 (hCRM1) in nuclear transport.

Main Methods:

  • Protein identification and cloning of CAN/Nup214-associated proteins.
  • Depletion studies using CAN/Nup214 knockdown.
  • Localization studies of Nup88 and hCRM1.
  • Analysis of CAN-/- mouse embryos.

Main Results:

  • Identified and cloned an 88 kDa protein, Nup88, a novel NPC component whose localization depends on CAN/Nup214.
  • Identified the 112 kDa protein as human CRM1 (hCRM1), a homolog of yeast CRM1, which localizes to the NPC and nucleoplasm.
  • Demonstrated that CAN/Nup214 is essential for hCRM1's NPC localization; hCRM1 interacts with the FG-repeat region of CAN/Nup214 and shares homology with importin-beta.

Conclusions:

  • CAN/Nup214 is essential for the NPC localization of Nup88 and hCRM1.
  • hCRM1 functions as a soluble nuclear transport factor interacting with the NPC, potentially via repeat-containing nucleoporins.
  • CAN/Nup214-Nup88 and CAN/Nup214-hCRM1 interactions are critical for nuclear transport and cellular integrity.

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