| First Author | Yano K | Year | 2011 |
| Journal | FEBS Lett | Volume | 585 |
| Issue | 6 | Pages | 841-6 |
| PubMed ID | 21349273 | Mgi Jnum | J:170708 |
| Mgi Id | MGI:4947170 | Doi | 10.1016/j.febslet.2011.02.020 |
| Citation | Yano K, et al. (2011) Functional significance of the interaction with Ku in DNA double-strand break recognition of XLF. FEBS Lett 585(6):841-6 |
| abstractText | Ku heterodimer is essential for the repair of DNA double-strand breaks (DSBs) by non-homologous end-joining (NHEJ). Ku recruits XLF, also known as Cernunnos, to DSBs. Here we report domain analyses of Ku-XLF interaction. The heterodimeric domain of Ku was found to be sufficient for the recruitment of XLF to DSBs and for the interaction of Ku with XLF. A small C-terminal deletion of XLF completely abolished recruitment of XLF to DSBs and Ku-XLF interaction. This deletion also led to marked reduction of XLF-XRCC4 interaction although the XRCC4-binding site on the XLF N-terminal domain remained intact. These results demonstrate the significance of Ku-XLF interaction in the molecular assembly of NHEJ factors. STRUCTURED SUMMARY OF PROTEIN INTERACTIONS: XLFphysically interacts with XRCC4 and Ku by anti tag coimmunoprecipitation(View interaction). |
