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

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.

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Publication Details

Journal
The EMBO Journal
Published
2025-10-02
DOI
https://doi.org/10.1038/s44318-025-00576-0
Primary Topic
PARP inhibition in cancer therapy
Type
article
Field-Weighted Citation Impact
0.00
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article

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

A.J. Middleton, Catherine L. Day
The EMBO Journal
PARP inhibition in cancer therapy
article

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

A.J. Middleton, Catherine L. Day
article en

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.

The EMBO JournalVol. 44(21)
University of Otago (NZ)
Openalex Percentile: Top 63%
PARP inhibition in cancer therapy
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