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Orchestration of the DNA-Damage Response by the RNF8 Ubiquitin Ligase

The cell response to -damage is manipulated by phosphorylation of and the ligase. N. K. Kolas, J. R. Chapman and S. Nakada from the Samuel Lunenfeld Research Institute in Canada and from the University of Cambridge (UK) discovered that is responsible for conjugation and the accumulation of and at locations of -damage.

The scientists state that recruits by phosphor-dependent interactions between the forkhead-associated domain of and motifs in that are phosphorylated by (a protein kinase activated upon -damage). Furthermore, the depletion of E2 enzyme UBC13 impairs the recruitment of to damaged , which points at a cooperation with . The researchers also observed that promotes the G2/M damage checkpoint and enhances resistance to ionising radiation. Recruiting of , and to sites of double-strand breaks has been observed before, but the mechanism of how the -damage response is orchestrated by -dependent phosphorylation of and -mediated ubiquitination has been unsolved until now.

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