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Related Concept Videos

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Attachment of Sister Chromatids

As cells progress into mitosis, the nuclear envelope breaks down, and the condensed chromosomes are exposed to the array of bipolar microtubules of the mitotic spindle. The kinetochore, a large, disc-shaped protein complex, is present at the centromere region of the sister chromatids and acts as a binding site for the microtubules.  Usually, the plus-end of a single microtubule is embedded within the kinetochore. However, some kinetochores first establish lateral contact with the side-wall of a...
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Real-Time Monitoring of Aurora kinase A Activation using Conformational FRET Biosensors in Live Cells
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Published on: July 30, 2020

Aurora A contributes to p150(glued) phosphorylation and function during mitosis.

Pierre Romé1, Emilie Montembault, Nathalie Franck

  • 1Centre National de la Recherche Scientifique UMR6061, Institut de Génétique et Dévelopement de Rennes, Université de Rennes, 35043 Rennes, France.

The Journal of Cell Biology
|May 19, 2010
PubMed
Summary

Aurora A kinase regulates cell division by phosphorylating the dynactin p150(glued) subunit. This phosphorylation limits dynactin-microtubule binding, ensuring proper spindle assembly and chromosome segregation during mitosis.

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Combining Mitotic Cell Synchronization and High Resolution Confocal Microscopy to Study the Role of Multifunctional Cell Cycle Proteins During Mitosis

Published on: December 5, 2017

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Genetics

Background:

  • Aurora A is a kinase crucial for mitotic spindle assembly and chromosome segregation.
  • Dynactin is a protein complex that interacts with microtubules and is involved in various cellular processes, including mitosis.

Purpose of the Study:

  • To investigate the role of Aurora A in regulating the localization and function of dynactin during mitosis.
  • To identify the specific interactions and phosphorylation events mediated by Aurora A on dynactin.

Main Methods:

  • Utilized Drosophila melanogaster as a model organism.
  • Employed biochemical assays to study protein phosphorylation and binding.
  • Investigated the effects of Aurora A inhibition on dynactin localization and function.

Main Results:

  • Aurora A phosphorylates the dynactin subunit p150(glued) on its microtubule-binding domain (MBD).
  • This phosphorylation is essential for regulating dynactin's association with mitotic spindle microtubules.
  • Compromised Aurora A function leads to aberrant enrichment of dynactin and dynein on spindle microtubules.

Conclusions:

  • Aurora A kinase controls dynactin-microtubule interactions through phosphorylation of the p150(glued) MBD.
  • This phosphoregulation is critical for limiting dynein-dynactin complex binding and ensuring accurate spindle assembly.
  • The findings elucidate a key mechanism by which Aurora A contributes to faithful chromosome segregation.