Activation of protein kinase C delta by the c-Abl tyrosine kinase in response to ionizing radiation

  • Oncogene. 1998 Apr 2;16(13):1643-8. doi: 10.1038/sj.onc.1201698.
Z M Yuan  1 T Utsugisawa T Ishiko S Nakada Y Huang S Kharbanda R Weichselbaum D Kufe
Affiliations
  • 1. Division of Cancer Pharmacology, Dana-Farber Cancer Institute, Harvard Medical School, Boston, Massachusetts 02115, USA.
Abstract

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.

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