Ku recruits XLF to DNA double‐strand breaks
Author:
Affiliation:
1. Division of Molecular Radiation Biology, Department of Radiation Oncology, University of Texas Southwestern Medical Center at Dallas 5801 Forest Park Road Dallas Texas 75390‐9187 USA
Publisher
EMBO
Subject
Genetics,Molecular Biology,Biochemistry
Link
https://onlinelibrary.wiley.com/doi/pdf/10.1038/sj.embor.7401137
Reference25 articles.
1. XLF Interacts with the XRCC4-DNA Ligase IV Complex to Promote DNA Nonhomologous End-Joining
2. Absence of DNA ligase IV protein in XR-1 cells: evidence for stabilization by XRCC4
3. Cernunnos, a Novel Nonhomologous End-Joining Factor, Is Mutated in Human Immunodeficiency with Microcephaly
4. Cernunnos Interacts with the XRCC4·DNA-ligase IV Complex and Is Homologous to the Yeast Nonhomologous End-joining Factor Nej1
5. Coordinated Assembly of Ku and p460 Subunits of the DNA-dependent Protein Kinase on DNA Ends is Necessary for XRCC4–ligase IV Recruitment
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2. Multivalent interactions of the disordered regions of XLF and XRCC4 foster robust cellular NHEJ and drive the formation of ligation-boosting condensates in vitro;Nature Structural & Molecular Biology;2024-06-19
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