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Related Experiment Videos

Bub2 is a cell cycle regulated phospho-protein controlled by multiple checkpoints.

Fenghua Hu1, Stephen J Elledge

  • 1Verna and Mars McLean Department of Biochemistry and Molecular Biology, Howard Hughes Medical Institute, Baylor College of Medicine, Houston, Texas 77030, USA.

Cell Cycle (Georgetown, Tex.)
|December 4, 2002
PubMed
Summary

Bub2 protein phosphorylation regulates mitotic exit by modulating the Bub2/Bfa1 GTPase activating complex (GAP). Spindle damage prevents Bub2 phosphorylation, indicating checkpoint control over this novel regulatory pathway.

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Genetics

Background:

  • Mitotic exit requires Tem1 GTPase activation, antagonized by the Bub2/Bfa1 GTPase activating complex (GAP).
  • Bfa1 phosphorylation by Cdc5 releases Tem1 inhibition, but additional regulation of the GAP complex is suggested.
  • The Bub2/Bfa1 GAP complex also prevents mitotic exit during cell cycle checkpoints.

Purpose of the Study:

  • To investigate the cell cycle-regulated phosphorylation of Bub2 protein.
  • To determine the role of Bub2 phosphorylation in regulating the Bub2/Bfa1 GAP complex activity.
  • To elucidate the upstream regulators of Bub2 phosphorylation, particularly in response to cell cycle checkpoints.

Main Methods:

  • Analysis of Bub2 protein phosphorylation during the cell cycle.

Related Experiment Videos

  • Investigating the dependence of Bub2 phosphorylation on the kinase Cdc5.
  • Assessing the impact of spindle damage and misorientation on Bub2 phosphorylation.
  • Examining the role of spindle assembly checkpoint components (Mad2, Mps1) in regulating Bub2 phosphorylation.

    • Main Results:

    • Bub2 protein exhibits cell cycle-regulated phosphorylation, partially dependent on Cdc5.
    • Bub2 phosphorylation is consistent with negative regulation of the Bub2/Bfa1 GAP complex.
    • Spindle damage or misorientation prevents Bub2 phosphorylation, dependent on Mad2 and Mps1.
    • These findings suggest Bub2 phosphorylation is controlled by a novel kinase.

    Conclusions:

    • Bub2, like Bfa1, is subject to regulation during mitotic exit and in response to cell cycle checkpoints.
    • Bub2 phosphorylation represents a novel mechanism for controlling the Bub2/Bfa1 GAP complex.
    • Further research is needed to identify the novel kinase responsible for Bub2 phosphorylation.