# RNF114, a RING E3 ligase that reads and extends the hybrid ADP-ribose-ubiquitin signal

## TL;DR

This paper explores how RNF114, an E3 ligase, recognizes and extends a hybrid ADP-ribose-ubiquitin modification, linking it to DNA repair and stress response.

## Contribution

The study identifies a novel domain in RNF114 that recognizes both ADP-ribose and ubiquitin, enabling further ubiquitination.

## Key findings

- RNF114 recognizes a hybrid ADP-ribose-ubiquitin modification on substrate proteins.
- RNF114 assembles Lys11-linked ubiquitin chains on this hybrid modification.
- This function positions RNF114 at the intersection of DNA repair and stress response pathways.

## Abstract

Post-translational modifications (PTMs) expand protein function and serve as key regulators of virtually all cellular processes. Several recent studies show that the E3 ligase RNF114 recognises a hybrid ADP-ribose-ubiquitin modification on substrate proteins and uses it as a platform to assemble Lys11-linked ubiquitin chains, placing RNF114 at the crossroads of DNA repair processes that help cells safeguard their genome and respond to stress.

Several recent studies report the characterization of a novel domain recognizing both ADPr and ubiquitin, enabling ubiquitin ligases to catalyze further modification of this posttranslational mark.