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Related Experiment Videos

The spindle checkpoint requires cyclin-dependent kinase activity.

Vincenzo D'Angiolella1, Cecilia Mari, Donatella Nocera

  • 1Dipartimento di Biologia e Patologia Molecolare e Cellulare L, Califano Medical School, University of Napoli, Federico II, Pansini 5, 80131 Napoli, Italy.

Genes & Development
|October 17, 2003
PubMed
Summary

Mitotic cyclin-dependent kinase (cdk) activity is essential for the spindle checkpoint to prevent premature cell division. Inhibiting cdk overrides the checkpoint, allowing cell cycle progression by releasing the APC/CCdc20 complex.

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Genetics

Background:

  • The spindle checkpoint is a critical cell cycle surveillance mechanism.
  • It ensures accurate chromosome segregation by preventing anaphase onset until all chromosomes are properly attached to the mitotic spindle.
  • This checkpoint restrains the anaphase-promoting complex/cyclosome-Cdc20 (APC/CCdc20), a ubiquitin ligase that triggers sister chromatid separation.

Purpose of the Study:

  • To investigate the role of mitotic cyclin-dependent kinase (cdk) activity in regulating the spindle checkpoint.
  • To determine how cdk activity influences the interaction between APC/CCdc20 and its regulators, such as Mad2.

Main Methods:

  • Experiments were conducted using Xenopus egg extracts and human cell lines.
  • Cyclin-dependent kinase (cdk) activity was inhibited using specific inhibitors.

Related Experiment Videos

  • Interactions between APC/C, Cdc20, and Mad2 were analyzed following cdk inhibition.
  • In vitro phosphorylation of Cdc20 by cdk1 was performed.

    • Main Results:

    • Spindle checkpoint-dependent mitotic arrest was overridden upon inhibition of cdk activity.
    • Inhibiting cdk led to a transient increase in the interaction between APC/C and Cdc20.
    • Mad2, an inhibitory checkpoint protein, dissociated from Cdc20 after cdk inhibition.
    • Cdk inhibition also effectively overcame Mad2-induced mitotic arrest.
    • In vitro studies showed that cdk1-phosphorylated Cdc20 interacts with Mad2, not APC/C.

    Conclusions:

    • Mitotic cdk activity is required for the spindle checkpoint to function correctly.
    • Cdk activity restrains the activation of APC/CCdc20 until the completion of mitotic spindle assembly.
    • Phosphorylation of Cdc20 by cdk1 appears to be a key mechanism for maintaining checkpoint control.