INACTIVATION OF BCL-2 BY PHOSPHORYLATION

被引:729
作者
HALDAR, S [1 ]
JENA, N [1 ]
CROCE, CM [1 ]
机构
[1] THOMAS JEFFERSON UNIV,JEFFERSON CANC CTR,PHILADELPHIA,PA 19107
关键词
APOPTOSIS; PROGRAMMED CELL DEATH; ONCOGENE; HUMAN CANCER; LIPID PEROXIDATION;
D O I
10.1073/pnas.92.10.4507
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
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.
引用
收藏
页码:4507 / 4511
页数:5
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