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Bcl-2 phosphorylation required for anti-apoptosis function

T Ito1, X Deng, B Carr

  • 1Sealy Center for Oncology and Hematology and Department of Internal Medicine, University of Texas Medical Branch, Galveston, Texas 77555-1048, USA.

The Journal of Biological Chemistry
|May 2, 1997
PubMed
Summary
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Phosphorylation of the proto-oncogene Bcl-2 is essential for its role in suppressing apoptosis. Mutating key phosphorylation sites impairs Bcl-2 function, demonstrating phosphorylation

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Oncology

Background:

  • The proto-oncogene Bcl-2 inhibits apoptosis in growth factor-dependent cells.
  • A post-receptor signaling mechanism for Bcl-2 function remained unknown.
  • Interleukin-3 (IL-3), erythropoietin, and bryostatin-1 (Bryo) suppress apoptosis and stimulate Bcl-2 phosphorylation.

Purpose of the Study:

  • To investigate whether Bcl-2 phosphorylation is required for its anti-apoptotic function.
  • To determine the role of specific protein kinase C phosphorylation sites in Bcl-2 activity.

Main Methods:

  • Conservative serine to alanine mutations were introduced at seven putative protein kinase C phosphorylation sites in Bcl-2.
  • The phosphorylation status and anti-apoptotic function of wild-type and mutant Bcl-2 were assessed.

Related Experiment Videos

  • Cell survival was evaluated under conditions of IL-3 deprivation and etoposide treatment.
  • Heterodimerization of Bcl-2 mutants with Bax was analyzed.

    • Main Results:

    • The S70A Bcl-2 mutant, lacking phosphorylation at serine 70, failed to suppress apoptosis upon IL-3 withdrawal or etoposide exposure.
    • The S70E mutant, mimicking a phosphate charge, enhanced suppression of etoposide-induced apoptosis.
    • The S70A mutant retained the ability to heterodimerize with Bax, indicating this interaction is insufficient for full function.

    Conclusions:

    • Bcl-2 phosphorylation, specifically at serine 70, is crucial for its full death suppressor activity.
    • Bcl-2:Bax heterodimerization alone is not sufficient to mediate Bcl-2's anti-apoptotic signaling.
    • Phosphorylation is a key post-translational modification regulating Bcl-2's role in cell survival.