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Related Experiment Videos

Aurora B phosphorylates centromeric MCAK and regulates its localization and microtubule depolymerization activity.

Weijie Lan1, Xin Zhang, Susan L Kline-Smith

  • 1Department of Biochemistry and Molecular Genetics, University of Virginia Medical School, Charlottesville, VA 22908, USA.

Current Biology : CB
|February 20, 2004
PubMed
Summary

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Aurora B kinase directly regulates mitotic centromere-associated kinesin (MCAK) activity through phosphorylation. This interaction is crucial for proper chromosome segregation during cell division, ensuring accurate cell division.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Genetics

Background:

  • Accurate chromosome segregation during mitosis relies on sister kinetochores binding microtubules in a bipolar fashion.
  • The precise molecular mechanisms governing this process, particularly the roles of Aurora B kinase and mitotic centromere-associated kinesin (MCAK), are not fully understood.
  • Both Aurora B and MCAK are localized to mitotic centromeres and share overlapping functions in regulating microtubule dynamics and correcting erroneous kinetochore-microtubule attachments.

Purpose of the Study:

  • To elucidate the regulatory relationship between Aurora B kinase and MCAK during mitosis.
  • To investigate how Aurora B influences MCAK's function in microtubule depolymerization and kinetochore-microtubule attachments.
  • To determine the functional significance of MCAK phosphorylation by Aurora B in chromosome biorientation.

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Main Methods:

  • In vitro and in vivo biochemical assays to study Aurora B-mediated phosphorylation of MCAK.
  • Mapping of Aurora B phosphorylation sites on MCAK.
  • Immunofluorescence microscopy to assess the localization of MCAK and phosphorylated MCAK.
  • Functional assays using Xenopus egg extracts and cell injections with antibodies targeting phosphorylated MCAK.

Main Results:

  • Aurora B directly phosphorylates MCAK at six sites, located in both the centromere-targeting domain and the neck region.
  • Aurora B activity is essential for MCAK localization to centromeres, but not spindle poles.
  • Phosphorylation of serine 196 in MCAK's neck region by Aurora B inhibits its microtubule depolymerization activity.
  • Phosphorylated MCAK was observed at centromeres and anaphase spindle midzones, with distinct pockets of phosphorylated and unphosphorylated MCAK within the inner centromere.
  • Inhibition of S196 phosphorylation led to defects in chromosome positioning and segregation.

Conclusions:

  • A direct regulatory link between Aurora B kinase and the microtubule depolymerase MCAK has been established.
  • Aurora B exerts both positive and negative regulatory control over MCAK during mitosis.
  • Aurora B likely promotes chromosome biorientation by modulating MCAK's depolymerase activity on incorrectly attached kinetochore microtubules.