Ubiquitin-A structural perspective
Author(s)
Agrata, R; Komander, D;
Details
Publication Year 2025-01-16,Volume 85,Issue #2,Page 323-346
Journal Title
Molecular Cell
Abstract
The modification of proteins and other biomolecules with the small protein ubiquitin has enthralled scientists from many disciplines for decades, creating a broad research field. Ubiquitin research is particularly rich in molecular and mechanistic understanding due to a plethora of (poly)ubiquitin structures alone and in complex with ubiquitin machineries. Furthermore, due to its favorable properties, ubiquitin serves as a model system for many biophysical and computational techniques. Here, we review the current knowledge of ubiquitin signals through a ubiquitin-centric, structural biology lens. We amalgamate the information from 240 structures in the Protein Data Bank (PDB), combined with single-molecule, molecular dynamics, and nuclear magnetic resonance (NMR) studies, to provide a comprehensive picture of ubiquitin and polyubiquitin structures and dynamics. We close with a discussion of the latest frontiers in ubiquitin research, namely the modification of ubiquitin by other post-translational modifications (PTMs) and the notion that ubiquitin is attached to biomolecules beyond proteins.
Publisher
Cell Press
Keywords
*Ubiquitin/metabolism/chemistry; Humans; *Protein Processing, Post-Translational; *Ubiquitination; Animals; Molecular Dynamics Simulation; Protein Conformation; Databases, Protein; Polyubiquitin/metabolism/chemistry; Protein Binding; Structure-Activity Relationship; linkage specificity; non-proteinaceous; phospho-ubiquitin; post-translational modification; ubiquitin; ubiquitin chain
Research Division(s)
Ubiquitin Signalling
PubMed ID
39824171
Terms of Use/Rights Notice
Refer to copyright notice on published article.


Creation Date: 2025-02-07 02:57:11
Last Modified: 2025-02-07 03:13:23
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