Yuan Z M, Utsugisawa T, Ishiko T, Nakada S, Huang Y, Kharbanda S, Weichselbaum R, Kufe D
Division of Cancer Pharmacology, Dana-Farber Cancer Institute, Harvard Medical School, Boston, Massachusetts 02115, USA.
Oncogene. 1998 Apr 2;16(13):1643-8. doi: 10.1038/sj.onc.1201698.
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 delta (PKCdelta). The results show that the SH3 domain of c-Abl interacts directly with PKCdelta. c-Abl phosphorylates and activates PKCdelta in vitro. We also show that IR treatment of cells is associated with c-Abl-dependent phosphorylation of PKCdelta and translocation of PKCdelta to the nucleus. These findings support a functional interaction between c-Abl and PKCdelta in the cellular response to genotoxic stress.
c-Abl蛋白酪氨酸激酶可被电离辐射（IR）及某些其他DNA损伤剂激活。目前的研究表明，c-Abl与蛋白激酶Cδ（PKCδ）持续结合。结果显示，c-Abl的SH3结构域直接与PKCδ相互作用。c-Abl在体外使PKCδ磷酸化并激活PKCδ。我们还表明，对细胞进行IR处理与PKCδ的c-Abl依赖性磷酸化以及PKCδ转位至细胞核有关。这些发现支持了c-Abl与PKCδ在细胞对遗传毒性应激反应中的功能相互作用。
