Chatrin

The rise of ADP-ribose–ubiquitin Nature Structural & Molecular Biology, Published online: 08 September 2025; doi:10.1038/s41594-025-01651-0Post-translational modifications show mechanistic crosstalk, exemplified by the ADP-ribose–ubiquitin hybrid signal, in which one post-translational modification modifies another. This Comment highlights its discovery, mechanistic basis and functional consequences, and outlines critical questions for understanding this emerging signaling paradigm.

ICYMI: New online: The rise of ADP-ribose–ubiquitin

Read our comment on the rise of ADP-ribose-Ubiquitin hybrid modification. It's been fun to see it grows :)

Identification of RNF114 as ADPr-Ub reader through non-hydrolysable ubiquitinated ADP-ribose - Nature Communications Deltex E3s modify ADP-ribosylated targets with ubiquitin, creating a hybrid modification whose readers remains unknown. Here, the authors synthesise a non-hydrolysable probe that mimics the modificati...

An amazing paper from van der Heden and Ahel groups! They use clever chemistry to identify RNF114 as a dual ADP-ribose-Ubiquitin reader involved in the DNA damage response! Congratulations to first authors Max, @chatrin-c.bsky.social and Rishov. Happy to have a small contribution in this story