| Literature DB >> 9582011 |
Z M Yuan1, T Utsugisawa, T Ishiko, S Nakada, Y Huang, S Kharbanda, R Weichselbaum, D Kufe.
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.Entities:
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Year: 1998 PMID: 9582011 DOI: 10.1038/sj.onc.1201698
Source DB: PubMed Journal: Oncogene ISSN: 0950-9232 Impact factor: 9.867