Inactivation of Bcl-2 by phosphorylation.

• S Haldar

  Jefferson Cancer Institute, Thomas Jefferson University, Philadelphia, PA 19107, USA.

• N Jena

  Jefferson Cancer Institute, Thomas Jefferson University, Philadelphia, PA 19107, USA.

• C M Croce

  Jefferson Cancer Institute, Thomas Jefferson University, Philadelphia, PA 19107, USA.

抄録

The antiapoptosis potential of Bcl-2 protein is well established, but the mechanism of Bcl-2 action is still poorly understood. Using the phosphatase inhibitor okadaic acid or the chemotherapeutic drug taxol, we found that Bcl-2 was phosphorylated in lymphoid cells. Phospho amino acid analysis revealed that Bcl-2 was phosphorylated on serine. Under similar conditions, okadaic acid or taxol treatment led to the induction of apoptosis in these cells. Thus, phosphorylation of Bcl-2 seems to inhibit its ability to interfere with apoptosis. In addition, phosphorylated Bcl-2 can no longer prevent lipid peroxidation as required to protect cells from apoptosis.

収録刊行物

• Proceedings of the National Academy of Sciences

  Proceedings of the National Academy of Sciences 92 (10), 4507-4511, 1995-05-09

  Proceedings of the National Academy of Sciences

キーワード

• Multidisciplinary

詳細情報

• CRID: 1362825895663662592
• NII論文ID: 80008309761
• DOI: 10.1073/pnas.92.10.4507
• ISSN: 10916490
• ISSN: 00278424
• Web Site: https://pnas.org/doi/pdf/10.1073/pnas.92.10.4507
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