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Aurora-C interacts with and phosphorylates the transforming acidic coiled-coil 1 protein

Jean-Charles Gabillard1, Salvatore Ulisse, Enke Baldini

  • 1CNRS-UMR 6061, Institut Génétique et Développement, IFR 140, UEB-Université Rennes 1, 2 Avenue du Pr Léon Bernard, Rennes Cedex, France.

Biochemical and Biophysical Research Communications
|May 3, 2011
PubMed

Insights

This study reveals that TACC1 protein interacts with Aurora-C kinase and localizes to the midbody during cell division. Aurora-C phosphorylates TACC1, suggesting a role in regulating cytokinesis.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Aurora-C kinase is involved in mitosis regulation but its functions remain unclear.
  • TACC1 protein, part of the transforming acidic coiled-coil family, interacts with Aurora kinases.

Purpose of the Study:

  • To investigate the interaction between Aurora-C and TACC1.
  • To characterize the cellular localization and functional relationship of Aurora-C and TACC1.

Main Methods:

  • Immunofluorescence (IF) for co-localization studies.
  • Co-immunoprecipitation (IP) to confirm protein association.
  • In vitro kinase assays to assess phosphorylation activity.

Main Results:

  • Aurora-C and TACC1 were found to co-localize at the midbody during HeLa cell cytokinesis.
  • TACC1 was successfully immunoprecipitated with Aurora-C from cell extracts.
  • Aurora-C was demonstrated to phosphorylate TACC1 at serine 228 in vitro.

Conclusions:

  • TACC1 localizes to the midbody during cytokinesis and interacts with Aurora-C.
  • TACC1 is a direct substrate of Aurora-C kinase.
  • This interaction warrants further investigation into its functional significance in cell division.

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