Activation of protein kinase C δ by the c-Abl tyrosine kinase in response to ionizing radiation
Activation of protein kinase C δ by the c-Abl tyrosine kinase in response to ionizing radiation
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DOI：
10.1038/sj.onc.1201698
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发表时间：
1998-04
期刊：
影响因子：
8
通讯作者：
Zhi-Min Yuan;T. Utsugisawa;T. Ishiko;S. Nakada;Yinyin Huang;S. Kharbanda;R. Weichselbaum;D. Kufe
中科院分区：
文献类型：
--
作者：
Zhi-Min Yuan;T. Utsugisawa;T. Ishiko;S. Nakada;Yinyin Huang;S. Kharbanda;R. Weichselbaum;D. Kufe
C-Abl蛋白酪氨酸激酶被电离辐射(IR)和某些其他DNA损伤剂激活。目前的研究表明，c-Abl与蛋白激酶Cδ(PKCδ)密切相关。结果表明，c-Abl的SH3结构域直接与PKCδ相互作用。C-Abl在体外磷酸化并激活蛋白激酶Cδ。我们还表明，细胞的IR处理与c-Abl依赖的蛋白激酶Cδ的磷酸化和蛋白激酶Cδ向细胞核的移位有关。这些发现支持c-Abl和PKCδ在细胞对遗传毒性应激的反应中存在功能上的相互作用。
The c-Abl protein tyrosine kinase is activated by ionizing radiation (IR) and certain other DNA-damaging agents. The present studies demonstrate that c-Abl associates constitutively with protein kinase C δ (PKCδ). The results show that the SH3 domain of c-Abl interacts directly with PKCδ. c-Abl phosphorylates and activates PKCδ in vitro. We also show that IR treatment of cells is associated with c-Abl-dependent phosphorylation of PKCδ and translocation of PKCδ to the nucleus. These findings support a functional interaction between c-Abl and PKCδ in the cellular response to genotoxic stress.