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Phosphorylation regulates the p31Comet-mitotic arrest-deficient 2 (Mad2) interaction to promote spindle assembly

Dipali A Date1, Amy C Burrows1, Matthew K Summers1

  • 1Department of Cancer Biology, Lerner Research Institute, Cleveland, Ohio 44195.

The Journal of Biological Chemistry
|March 6, 2014
PubMed

Insights

p31(Comet) inhibits the spindle assembly checkpoint (SAC) by binding Mad2. Phosphorylation of p31(Comet) weakens this interaction, promoting SAC activity and accurate cell division.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Genetics

Background:

  • The spindle assembly checkpoint (SAC) is crucial for accurate chromosome segregation during mitosis.
  • p31(Comet) acts as a negative regulator of the SAC by interacting with Mad2, promoting mitotic progression.

Purpose of the Study:

  • To investigate the regulatory mechanism of p31(Comet) interaction with Mad2.
  • To determine how p31(Comet) influences SAC activity during mitosis.

Main Methods:

  • Co-immunoprecipitation assays to study protein-protein interactions.
  • Site-directed mutagenesis to investigate the role of specific phosphorylation sites.
  • Cell-based assays to monitor SAC activity and mitotic progression.

Main Results:

  • p31(Comet) binds Mad2 exclusively in an inhibitory capacity.
  • Phosphorylation of p31(Comet) at Ser-102 reduces its affinity for Mad2.
  • This phosphorylation event enhances p31(Comet)-mediated bypass of the SAC, promoting mitotic progression.

Conclusions:

  • p31(Comet) activity is regulated by phosphorylation, providing a novel mechanism for controlling SAC function.
  • This study reveals a previously unrecognized regulatory event impacting SAC activity and genome stability.
Keywords:
Anaphase-promoting ComplexCell CycleCell DivisionMad2MitosisMitotic Checkpoint ComplexProtein ComplexesProtein PhosphorylationSpindle Assembly Checkpointp31Comet

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