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Related Experiment Videos

Entry into mitosis without Cdc2 kinase activation

P M Gowdy1, H J Anderson, M Roberge

  • 1Department of Biochemistry and Molecular Biology, University of British Columbia, Vancouver, BC, Canada, V6T 1Z3.

Journal of Cell Science
|October 28, 1998
PubMed
Summary
This summary is machine-generated.

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Okadaic acid triggers key mitotic events like chromosome condensation and nuclear lamina breakdown in cells lacking Cdc2 kinase activity. This highlights the crucial roles of other kinases and phosphatases in initiating cell division.

Area of Science:

  • Cell Biology
  • Molecular Biology

Background:

  • Mouse FT210 cells arrest in G2 phase at 39°C due to absent Cdc2 kinase activity.
  • Okadaic acid, a protein phosphatase 1 and 2A inhibitor, induces chromosome condensation in these arrested cells.

Purpose of the Study:

  • To investigate the effects of okadaic acid on other early mitotic events in the absence of Cdc2 kinase activity.
  • To identify kinases and phosphatases involved in mitotic entry independent of Cdc2.

Main Methods:

  • Utilizing temperature-sensitive mouse FT210 cells arrested in G2 phase.
  • Employing okadaic acid to induce mitotic events.
  • Performing in-gel kinase assays and immunoprecipitation studies.

Main Results:

  • Okadaic acid induced nuclear lamina depolymerization and centrosome separation without Cdc2 kinase activity.

Related Experiment Videos

  • Mitotic entry was associated with partial Cdc25C activation and was inhibited by tyrosine phosphatase inhibitors and staurosporine.
  • A novel 45-kDa protein kinase, activated independently of Cdc2, was identified.

    • Conclusions:

    • Tyrosine phosphatases (like Cdc25C) and kinases other than Cdc2 are essential for structural changes during mitosis.
    • Cell entry into mitosis involves the coordinated activation of multiple kinases, including Cdc2 kinase.