The transforming acidic coiled coil proteins interact with nuclear histone acetyltransferases

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Omkaram Gangisetty1, Brenda Lauffart, Gautam V Sondarva

  • 1Department of Cancer Genetics, Roswell Park Cancer Institute, Elm and Carlton Streets, Buffalo, NY 14263, USA.

Oncogene
|February 10, 2004
PubMed

Insights

Transforming acidic coiled coil (TACC) proteins interact with histone acetyltransferase (HAT) hGCN5L2. This discovery suggests TACC proteins may influence gene regulation and contribute to cancer development.

Area of Science:

  • Molecular Biology
  • Cancer Research
  • Epigenetics

Background:

  • Dysregulation of transforming acidic coiled coil (TACC) genes is linked to multiple myeloma, breast, and gastric cancers.
  • The precise mechanisms of TACC protein function in cell growth and differentiation remain unclear.

Purpose of the Study:

  • To identify proteins that interact with TACC proteins.
  • To elucidate the functional relationship between TACC proteins and chromatin remodeling complexes.

Main Methods:

  • Yeast two-hybrid assay to identify TACC2-binding proteins.
  • GST pull-down assays to confirm in vitro binding of TACC family members to hGCN5L2.
  • Coimmunoprecipitation assays in HEK293 cells to validate interactions in a human cellular context.

Main Results:

  • The histone acetyltransferase (HAT) hGCN5L2 was identified as a TACC2-binding protein.
  • All human TACC family members demonstrated in vitro binding to hGCN5L2.
  • TACC2s isoform was found to be consistently bound to multiple HAT family members in HEK293 cells.

Conclusions:

  • TACC proteins interact with histone acetyltransferase (HAT) proteins, including hGCN5L2.
  • These interactions suggest a role for TACC proteins in gene regulation via chromatin remodeling complexes.
  • Aberrant TACC protein expression may contribute to tumorigenesis through altered gene regulation.

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