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Real-Time Monitoring of Aurora kinase A Activation using Conformational FRET Biosensors in Live Cells
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Tousled-mediated activation of Aurora B kinase does not require Tousled kinase activity in vivo

Gary M Riefler1, Sharon Y R Dent, Jill M Schumacher

  • 1Department of Molecular Genetics, M.D Anderson Cancer Center, University of Texas, Houston, Texas 77030, USA.

The Journal of Biological Chemistry
|March 13, 2008
PubMed

Insights

Tousled-like kinase (TLK) activates Aurora B kinase, a crucial protein for cell division. This study shows TLK functions independently of its kinase activity to enhance Aurora B activity in vivo.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Genetics

Background:

  • Aurora kinases are essential for cell division, regulating spindle assembly, chromosome segregation, and cytokinesis.
  • Some Aurora kinase substrates can enhance kinase activity upon phosphorylation.
  • Previous research indicated TLK-1 as a substrate and in vitro activator of AIR-2 Aurora B kinase.

Purpose of the Study:

  • To demonstrate that TLK-1 expression is sufficient for Aurora B activation in vivo.
  • To elucidate the in vivo relationship between Aurora B and Tousled kinases.

Main Methods:

  • Heterologous expression of wild-type and kinase-inactive TLK-1 in yeast.
  • Assessment of TLK-1's effect on the lethality of temperature-sensitive yeast Aurora B kinase (Ipl1) mutants.
  • Analysis of kinase-dead TLK-1 association with and augmentation of Ipl1 activity in vivo.

Main Results:

  • Heterologous expression of TLK-1, including kinase-inactive forms, rescued the lethality of yeast Ipl1 mutants.
  • Kinase-dead TLK-1 was found to associate with and enhance Ipl1 activity in vivo.
  • These findings provide evidence for a kinase-independent role of TLK in Aurora B activation.

Conclusions:

  • Tousled-like kinase plays a bona fide, kinase-independent role in activating Aurora B kinases in vivo.
  • This discovery deepens the understanding of cell division regulation and kinase-substrate interactions.

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