| First Author | Cao C | Year | 2003 |
| Journal | J Biol Chem | Volume | 278 |
| Issue | 15 | Pages | 12961-7 |
| PubMed ID | 12569093 | Mgi Jnum | J:82954 |
| Mgi Id | MGI:2656128 | Doi | 10.1074/jbc.M300058200 |
| Citation | Cao C, et al. (2003) Functional Interaction between the c-Abl and Arg Protein-tyrosine Kinases in the Oxidative Stress Response. J Biol Chem 278(15):12961-7 |
| abstractText | The Abl family of mammalian nonreceptor tyrosine kinases consists of c-Abl and Arg. Recent work has shown that c-Abl and Arg are activated in the cellular response to oxidative stress. The present studies demonstrate that reactive oxygen species (ROS) induce the formation of c-Abl and Arg heterodimers. The results show that the c-Abl SH3 domain binds directly to a proline-rich site (amino acids 567-576) in the Arg C-terminal region. Formation of c-Abl.Arg heterodimers also involves direct binding of the Arg Src homology 3 domain to the C-terminal region of c-Abl. The results further demonstrate that the interaction between c-Abl and Arg involves c-Abl-mediated phosphorylation of Arg. The functional significance of the c-Abl-Arg interaction is supported by the demonstration that both c-Abl and Arg are required for ROS-induced apoptosis. These findings indicate that ROS induce c-Abl.Arg heterodimers and that both c-Abl and Arg are necessary as effectors in the apoptotic response to oxidative stress. |
