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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Posttranslational myristoylation of caspase-activated p21-activated protein kinase 2 (PAK2) potentiates late apoptotic events
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Posttranslational myristoylation of caspase-activated p21-activated protein kinase 2 (PAK2) potentiates late apoptotic events

机译：caspase激活的p21激活的蛋白激酶2（PAK2）的翻译后肉豆蔻酰化可增强晚期凋亡事件。

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摘要

p21-activated protein kinase (PAK) 2 is a small GTPase-activated serine/threonine kinase regulating various cytoskeletal functions and is cleaved by caspase-3 during apoptosis. We demonstrate that the caspase-cleaved PAK2 C-terminal kinase fragment (C-t-PAK2) is posttranslationally myristoylated, although myristoylation is typically a cotranslational process. Myristoylation and an adjacent polybasic domain of C-t-PAK2 are sufficient to redirect EGFP from the cytosol to membrane ruffles and internal membranes. Membrane localization and the ability of C-t-PAK2 to induce cell death are significantly reduced when myristoylation is abolished. In addition, the proper myristoylation-dependent membrane localization of C-t-PAK2 significantly increased signaling through the stress-activated c-Jun N-terminal kinase signaling pathway, which often regulates apoptosis. Interestingly, C-t-PAK2 promoted cell death without compromising mitochondrial integrity. Posttranslational myristoylation of caspase-cleaved proteins involved in cytoskeletal dynamics (e.g., PAK2, actin, and gelsolin) might be part of a unique series of mechanisms involved in the regulation of the later events of apoptosis.
机译：p21激活的蛋白激酶（PAK）2是一种小的GTPase激活的丝氨酸/苏氨酸激酶，调节各种细胞骨架功能，并在凋亡过程中被caspase-3裂解。我们证明胱天蛋白酶切割的PAK2 C末端激酶片段（C-t-PAK2）是翻译后肉豆蔻酰化的，尽管肉豆蔻酰化通常是一个共翻译过程。 C-t-PAK2的肉豆蔻酰化和邻近的多元结构域足以将EGFP从胞质溶胶重定向到膜褶和内膜。取消肉豆蔻酰化后，膜的定位和C-t-PAK2诱导细胞死亡的能力大大降低。此外，C-t-PAK2的适当的肉豆蔻酰化依赖性膜定位可通过应激激活的c-Jun N端激酶信号传导途径显着增加信号传导，该通路通常调节细胞凋亡。有趣的是，C-t-PAK2可促进细胞死亡，而不会损害线粒体的完整性。参与细胞骨架动力学的caspase裂解蛋白的翻译后肉豆蔻酰化作用（例如PAK2，肌动蛋白和凝溶胶蛋白）可能是调控细胞凋亡后期事件的一系列独特机制的一部分。

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