We show that the E3 ubiquitin ligase DTX2 creates a dual hybrid ADP-ribosyl-ubiquitin mark (ADPr-Ub) at DNA damage sites, driving the recruitment of RNF114, RNF138, and RNF166 proteins independently of HPF1.
journals.plos.org/plosbiology/...
Recent studies have shown that ADP-ribose modifications can be further modified by ubiquitin (ADPr-Ub), but there are still major gaps in our knowledge around this modification and its role in the DNA damage response. This study biochemically characterises the amino acid specificity for ADPr-Ub production and its recognition by E3 ubiquitin ligases.