| Autor: |
Kumar, S, Pandey, P, Bharti, A, Jin, S, Weichselbaum, R, Weaver, D, Kufe, D, Kharbanda, S |
| Zdroj: |
Journal of Biological Chemistry; October 1998, Vol. 273 Issue: 40 p25654-8, 5p |
| Abstrakt: |
The Src-like protein-tyrosine kinase Lyn is activated by ionizing radiation and certain other DNA-damaging agents, whereas the DNA-dependent protein kinase (DNA-PK), consisting of the catalytic subunits (DNA-PKcs) and Ku DNA-binding components, requires DNA double-stranded breaks for activation. Here we demonstrate that Lyn associates constitutively with DNA-PKcs. The SH3 domain of Lyn interacts directly with DNA-PKcs near a leucine zipper homology domain. We also show that Lyn phosphorylates DNA-PKcs but not Ku in vitro. The interaction between Lyn and DNA-PKcs inhibits DNA-PKcs activity and the ability of DNA-PKcs to form a complex with Ku/DNA. These results support the hypothesis that there are functional interactions between Lyn and DNA-PKcs in the response to DNA damage. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
|
