From molecular logic to therapeutic modulation: advances in Ub/UBL signalling

Benjamin M. Foster; Chiara Maniaci

doi:10.1042/EBC20250062

From molecular logic to therapeutic modulation: advances in Ub/UBL signalling

Benjamin M. Foster (Lead / Corresponding author)
, Chiara Maniaci

MRC PPU

Research output: Contribution to journal › Editorial › peer-review

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Abstract

Ubiquitin (Ub) and ubiquitin-like proteins (UBLs) are central regulators of cell signalling, with roles spanning proteasomal degradation, immune defence, DNA repair, autophagy, and the stress response. Their conserved β-grasp fold provides a remarkably versatile protein architecture that can be redeployed across diverse signalling pathways and modulated in disease contexts. Conjugation and removal through dedicated E1-E2-E3 and protease systems generate a rich regulatory code, further diversified by chain topology, hybrid architectures, and emerging non-canonical modifications. This special issue highlights recent advances in Ub and UBL biology, from specialised UBL pathways to host-pathogen interactions and non-protein conjugation events, as well as translational applications such as targeted protein degradation. Together, these reviews showcase the breadth, adaptability, and therapeutic potential of these small but powerful modifiers.

Original language	English
Article number	EBC20250062
Number of pages	4
Journal	Essays in Biochemistry
Volume	69
Issue number	4
DOIs	https://doi.org/10.1042/EBC20250062
Publication status	Published - 24 Feb 2026

Keywords

post translational modification
therapeutics
ubiquitin signalling

ASJC Scopus subject areas

Biochemistry
Molecular Biology

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10.1042/EBC20250062Licence: CC BY

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title = "From molecular logic to therapeutic modulation: advances in Ub/UBL signalling",

abstract = "Ubiquitin (Ub) and ubiquitin-like proteins (UBLs) are central regulators of cell signalling, with roles spanning proteasomal degradation, immune defence, DNA repair, autophagy, and the stress response. Their conserved β-grasp fold provides a remarkably versatile protein architecture that can be redeployed across diverse signalling pathways and modulated in disease contexts. Conjugation and removal through dedicated E1-E2-E3 and protease systems generate a rich regulatory code, further diversified by chain topology, hybrid architectures, and emerging non-canonical modifications. This special issue highlights recent advances in Ub and UBL biology, from specialised UBL pathways to host-pathogen interactions and non-protein conjugation events, as well as translational applications such as targeted protein degradation. Together, these reviews showcase the breadth, adaptability, and therapeutic potential of these small but powerful modifiers.",

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AB - Ubiquitin (Ub) and ubiquitin-like proteins (UBLs) are central regulators of cell signalling, with roles spanning proteasomal degradation, immune defence, DNA repair, autophagy, and the stress response. Their conserved β-grasp fold provides a remarkably versatile protein architecture that can be redeployed across diverse signalling pathways and modulated in disease contexts. Conjugation and removal through dedicated E1-E2-E3 and protease systems generate a rich regulatory code, further diversified by chain topology, hybrid architectures, and emerging non-canonical modifications. This special issue highlights recent advances in Ub and UBL biology, from specialised UBL pathways to host-pathogen interactions and non-protein conjugation events, as well as translational applications such as targeted protein degradation. Together, these reviews showcase the breadth, adaptability, and therapeutic potential of these small but powerful modifiers.

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From molecular logic to therapeutic modulation: advances in Ub/UBL signalling

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