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Phosphorylation of BAD at Ser-128 during mitosis and paclitaxel-induced apoptosis

Maria Berndtsson1, Yoshiyuki Konishi, Azad Bonni

  • 1Cancer Center Karolinska, Department of Oncology-Pathology, Karolinska Institute, Stockholm, Sweden.

FEBS Letters
|May 24, 2005
PubMed

Insights

Phosphorylation of BAD at Serine 128 has cell-specific effects on apoptosis. While it promotes apoptosis in neurons, it does not in proliferating non-neural cells during mitosis or taxol treatment.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • The BCL-2 family member BAD regulates apoptosis through phosphorylation.
  • Phosphorylation at Serine 128 (BAD-S128) was recently identified to enhance BAD's apoptotic activity.

Purpose of the Study:

  • To investigate the cell-specific effects of BAD Serine 128 phosphorylation on apoptosis.
  • To determine if BAD-S128 phosphorylation occurs during mitosis and in response to taxol treatment.

Main Methods:

  • Western blotting to detect BAD-S128 phosphorylation in NIH3T3 cells during mitosis.
  • Analysis of BAD-S128 phosphorylation in taxol-treated mouse fibroblasts and MDA-MB-231 cells.
  • Utilizing a phosphorylation-defective dominant-negative BAD mutant to assess its effect on taxol-induced apoptosis.

Main Results:

  • BAD becomes phosphorylated at Ser-128 during the mitotic phase in NIH3T3 cells.
  • BAD-S128 phosphorylation is observed in taxol-treated mouse fibroblasts and human breast cancer cells.
  • A phosphorylation-defective BAD mutant did not inhibit taxol-induced apoptosis in these cells.

Conclusions:

  • BAD Serine 128 phosphorylation exhibits cell-specific roles in apoptosis regulation.
  • This phosphorylation event induces apoptosis in neuronal cells but not in proliferating non-neural cells during mitosis or taxol exposure.

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