INACTIVATION OF BCL-2 BY PHOSPHORYLATION
INACTIVATION OF BCL-2 BY PHOSPHORYLATION
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DOI：
10.1073/pnas.92.10.4507
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发表时间：
1995-05-09
影响因子：
11.1
通讯作者：
CROCE, CM
中科院分区：
文献类型：
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作者：
HALDAR, S;JENA, N;CROCE, CM
Bcl-2 蛋白的抗凋亡潜力已得到充分证实，但 Bcl-2 的作用机制仍知之甚少。使用磷酸酶抑制剂冈田酸或化疗药物紫杉醇，我们发现Bcl-2在淋巴细胞中被磷酸化。磷酸氨基酸分析显示 Bcl-2 在丝氨酸上被磷酸化。在类似条件下，冈田酸或紫杉醇处理导致这些细胞凋亡的诱导。因此，Bcl-2 的磷酸化似乎抑制了其干扰细胞凋亡的能力。此外，磷酸化的 Bcl-2 不再能够阻止保护细胞免于凋亡所需的脂质过氧化。
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.