PMID: 9461559 RLIMS-P 3 Check other iTextMine results Issue Report
Title
| 1. | Regulation of Rad51 function by c-Abl in response to DNA damage. |
Abstract
| 2. | The Rad51 protein, a homolog of bacterial RecA, functions in DNA double-strand break repair and genetic recombination. |
| 3. | Whereas Rad51 catalyzes ATP-dependent pairing and strand exchange between homologous DNA molecules, regulation of this function is unknown. |
| 4. | The c-Abl tyrosine kinase is activated by ionizing radiation and certain other DNA-damaging agents. |
| 5. | Here we demonstrate that c-Abl interacts constitutively with Rad51. |
| 6. | We show that c-Abl phosphorylates Rad51 on Tyr-54 in vitro. |
| 7. | The results also show that treatment of cells with ionizing radiation induces c-Abl-dependent phosphorylation of Rad51. |
| 8. | Phosphorylation of Rad51 by c-Abl inhibits the binding of Rad51 to DNA and the function of Rad51 in ATP-dependent DNA strand exchange reactions. |
| 9. | These findings represent the first demonstration that Rad51 is regulated by phosphorylation and support a functional role for c-Abl in regulating Rad51-dependent recombination in the response to DNA damage. |
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