Transforming acidic coiled-coil 3 and Aurora-A interact in human thyrocytes and their expression is deregulated in

Salvatore Ulisse1, Enke Baldini, Matteo Toller

  • 1Department of Experimental Medicine, University of Rome La Sapienza, Rome, Italy.

Endocrine-Related Cancer
|October 5, 2007
PubMed

Insights

Transforming acidic coiled-coil 3 (TACC3) expression is altered in thyroid cancer. Aurora-A kinase interacts with TACC3, influencing mitotic spindle organization crucial for cell division.

Area of Science:

  • Oncology
  • Molecular Biology
  • Cell Biology

Background:

  • Aurora-A kinase is deregulated in thyroid cancer.
  • Transforming acidic coiled-coil 3 (TACC3), an Aurora-A substrate, is vital for cell cycle progression and its expression changes in various cancers.

Purpose of the Study:

  • To investigate TACC3 gene expression in normal and cancerous thyroid cells and tissues.
  • To explore the relationship between TACC3, Aurora-A kinase, and mitotic spindle organization in thyroid cells.

Main Methods:

  • Quantitative analysis of TACC3 mRNA and protein levels in thyroid cell lines and patient tissues.
  • In vivo co-immunoprecipitation to assess TACC3 and Aurora-A interaction.
  • Immunofluorescence microscopy to determine protein localization.
  • Pharmacological inhibition of Aurora kinase activity.

Main Results:

  • TACC3 expression was significantly reduced in anaplastic, follicular, and papillary thyroid carcinoma cell lines compared to normal thyroid cells.
  • TACC3 mRNA levels were reduced in 56% and increased in 44% of differentiated thyroid cancer tissues.
  • A correlation between TACC3 and Aurora-A mRNA expression was observed in thyroid cancer tissues.
  • TACC3 and Aurora-A interact in vivo and localize to the mitotic spindle; TACC3 localization depends on Aurora kinase activity.

Conclusions:

  • TACC3 expression is dysregulated in thyroid cancer.
  • The interaction between Aurora-A kinase and TACC3 is crucial for proper mitotic spindle organization and chromosome segregation in thyroid cells.

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