Related Experiment Video

Updated: Aug 23, 2025

Real-Time Monitoring of Aurora kinase A Activation using Conformational FRET Biosensors in Live Cells
06:29

Real-Time Monitoring of Aurora kinase A Activation using Conformational FRET Biosensors in Live Cells

Published on: July 30, 2020

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Increased Aurora B expression reduces substrate phosphorylation and induces chromosomal instability

Eric M C Britigan1, Jun Wan2, Daniel K Sam3

  • 1Molecular and Cellular Pharmacology Graduate Training Program, University of Wisconsin-Madison, Madison, WI, United States.

Frontiers in Cell and Developmental Biology
|October 31, 2022
PubMed

Insights

High Aurora B protein levels paradoxically decrease its activity by disrupting essential complexes. This finding challenges the assumption that more Aurora B protein always means higher kinase function, impacting cancer research.

Area of Science:

  • Cell Biology
  • Molecular Oncology

Background:

  • Aurora B kinase is crucial for cell division.
  • Elevated Aurora B expression is observed in various cancers.
  • Increased Aurora B is typically associated with enhanced kinase activity and oncogenesis.

Purpose of the Study:

  • To investigate the functional consequences of increased Aurora B protein expression.
  • To determine the relationship between Aurora B expression levels and its kinase activity.
  • To explore the underlying mechanisms for observed effects.

Main Methods:

  • Studied Aurora B protein expression and its impact on substrate phosphorylation across three species.
  • Investigated the role of INCENP (Inner Centromere Protein) in Aurora B activation and localization.
  • Utilized co-expression strategies to rescue Aurora B activity.

Main Results:

  • Elevated Aurora B expression led to reduced phosphorylation of its substrates, mimicking inhibition.
  • Increased Aurora B caused mislocalization of INCENP, impairing complex formation and activation.
  • Co-expression of INCENP restored Aurora B kinase activity and mitigated mitotic defects.
  • Breast cancer data showed INCENP is not co-elevated with Aurora B.
  • Increased Aurora B conferred resistance to Aurora B inhibitors.

Conclusions:

  • Contrary to expectations, increased Aurora B protein expression reduces Aurora B kinase activity.
  • Proper localization and complex formation with INCENP are critical for Aurora B activation.
  • The findings have implications for cancer therapy and understanding Aurora B regulation.
Keywords:
CINaurora kinase inhibitormitosismitotic checkpointspindle assembly checkpoint

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