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MPF localization is controlled by nuclear export

A Hagting1, C Karlsson, P Clute

  • 1Wellcome/CRC Institute and Department of Zoology, Tennis Court Road, Cambridge, CB2 1QR, UK.

The EMBO Journal
|July 22, 1998
PubMed
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M phase promoting factor (MPF) shuttles between the nucleus and cytoplasm in interphase animal cells. Rapid nuclear export retains most MPF in the cytoplasm, regulating cell cycle progression.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Mitosis initiation in eukaryotes relies on M phase promoting factor (MPF), a complex of B-type cyclins and CDK1.
  • In animal cells, MPF resides in the cytoplasm during interphase and translocates to the nucleus post-mitosis initiation.

Purpose of the Study:

  • To investigate the dynamic behavior and localization of human cyclin B1 and MPF in living cells using real-time imaging.
  • To elucidate the mechanisms governing MPF nuclear import and export during the cell cycle.

Main Methods:

  • Utilized a fusion protein of human cyclin B1 and green fluorescent protein (GFP) for live-cell imaging.
  • Injected cyclin B1-GFP and MPF into interphase nuclei and observed their localization.
  • Employed leptomycin B to investigate the role of exportin 1 (CRM1) in nuclear export.

Related Experiment Videos

  • Studied the effect of a nuclear export signal-defective cyclin B1 mutant.

    • Main Results:

    • Injected cyclin B1-GFP and MPF were rapidly exported from the nucleus to the cytoplasm.
    • Nuclear export of cyclin B1 was inhibited by leptomycin B, implicating exportin 1 (CRM1).
    • A nuclear export sequence within cyclin B1 mediates MPF nuclear export, with defective mutants accumulating in interphase nuclei.
    • MPF exhibits continuous nucleocytoplasmic shuttling, with rapid export maintaining cytoplasmic retention.

    Conclusions:

    • MPF localization is actively regulated by CRM1-mediated nuclear export during interphase.
    • Defective nuclear export of cyclin B1 impacts MPF's role in cell cycle regulation, affecting sensitivity to CDK1 phosphorylation and Wee1 kinase inhibition.