| First Author | Imam SZ | Year | 2007 |
| Journal | Nucleic Acids Res | Volume | 35 |
| Issue | 15 | Pages | 4941-51 |
| PubMed ID | 17626041 | Mgi Jnum | J:172188 |
| Mgi Id | MGI:5004801 | Doi | 10.1093/nar/gkm386 |
| Citation | Imam SZ, et al. (2007) Cockayne syndrome protein B interacts with and is phosphorylated by c-Abl tyrosine kinase. Nucleic Acids Res 35(15):4941-51 |
| abstractText | The Cockayne Syndrome group B (CSB) protein plays important roles in transcription, transcription-coupled nucleotide excision repair and base excision DNA repair. c-Abl kinase also plays a role in DNA repair as a regulator/coordinator of the DNA damage response. This study presents evidence that the N-terminal region of CSB interacts with the SH3 domain of c-Abl in vitro and in vivo. In addition, c-Abl kinase phosphorylates CSB at Tyr932. The subcellular localization of CSB to the nucleus and nucleolus is altered after phosphorylation by c-Abl. c-Abl-dependent phosphorylation of CSB increased in cells treated with hydrogen peroxide and decreased in cells pre-treated with STI-571, a c-Abl-specific protein kinase inhibitor. Activation of the c-Abl kinase in response to oxidative damage is not observed in CSB null cells. These results suggest that c-Abl and CSB may regulate each other in a reciprocal manner in response to oxidative stress. |
