Protein phosphatase type 2C dephosphorylates BAD
Protein phosphatase type 2C dephosphorylates BAD
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DOI：
10.1016/s0197-0186(02)00174-2
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发表时间：
2003-06-01
影响因子：
4.2
通讯作者：
Krieglstein, J
中科院分区：
文献类型：
--
作者：
Klumpp, S;Selke, D;Krieglstein, J
可逆磷酸化调节细胞对凋亡的敏感性。BAD是Bcl-2蛋白家族的一员，其磷酸化状态是决定生命或死亡的重要检查点：BAD上丝氨酸残基112、136和155的磷酸化可防止细胞凋亡。在这里，我们报道BAD是PP2C的底物。Ser（155）参与了Bcl-X-L的异源二聚化。我们可以证明PP1， PP2A和PP2C在体外作用于该位点。然而，与BAD的P-Ser（112）和P-Ser（136）相比，只有PP2C优先考虑P-Ser（155）。结果表明，PP2C是触发BAD促凋亡功能的另一个因素。2003爱思唯尔科学有限公司版权所有。
Reversible phosphorylation modulates a cells' susceptibility to apoptosis. The phosphorylation status of BAD, a member of the Bcl-2 protein family, is an important checkpoint governing life-or-death decisions: Phosphorylation of serine residues 112, 136 and 155 on BAD prevents apoptosis. Here we report that BAD is a substrate for PP2C. Ser(155) is involved in heterodimerization with Bcl-X-L. We could demonstrate that PP1, PP2A and PP2C act on this site in vitro. However, only PP2C gives priority to P-Ser(155) compared to P-Ser(112) and P-Ser(136) on BAD. The results indicate that PP2C is an additional factor triggering the pro-apoptotic function of BAD. (C) 2003 Elsevier Science Ltd. All rights reserved.