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Aurora A orchestrates entosis by regulating a dynamic MCAK-TIP150 interaction.

Peng Xia1, Jinhua Zhou1, Xiaoyu Song1

  • 1Anhui Key Laboratory of Cellular Dynamics & Chemical Biology, Department of Optics and Optical Engineering, and Hefei National Laboratory for Physical Sciences at Nanoscale, University of Science and Technology of China, Hefei 230027, China.

Journal of Molecular Cell Biology
|May 22, 2014
PubMed
Summary

Microtubule plus-end-tracking protein TIP150 and MCAK cooperate to control cell-in-cell entosis. Aurora A phosphorylation of MCAK modulates this interaction, affecting cell rigidity and microtubule dynamics during division.

Keywords:
Aurora AMCAKTIP150entosiskinesinmicrotubule plus-end

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biophysics

Background:

  • Entosis, a cell-in-cell phenomenon, is linked to aneuploidy and aberrant cell division.
  • Microtubule plus-end-tracking protein TIP150 and MCAK are crucial for microtubule dynamics during cell division.

Purpose of the Study:

  • To investigate the regulatory mechanism of entosis involving TIP150, MCAK, and Aurora A.
  • To elucidate the role of MCAK-TIP150 interaction in regulating microtubule plasticity and cell mechanics during entosis.

Main Methods:

  • Biochemical analyses to study protein interactions.
  • In vitro phosphorylation assays using Aurora A.
  • Optical trap measurements of live cell mechanical rigidity (MCF7 cells).

Main Results:

  • TIP150 and MCAK cooperate to govern entosis.
  • Aurora A-mediated phosphorylation of MCAK disrupts the MCAK-TIP150 interaction, inhibiting entosis.
  • The MCAK-TIP150 interaction promotes microtubule dynamics and modulates cell rigidity during entosis.

Conclusions:

  • A regulatory circuitry involving Aurora A, MCAK, and TIP150 controls entosis.
  • Dynamic regulation of microtubule plasticity and cell rigidity by the MCAK-TIP150 complex is essential for entosis.
  • This study reveals a novel Aurora A regulatory mechanism in cell-in-cell processes.