Using Ubiquitin Binders to Decipher the Ubiquitin Code.
TUBE
affimers
autophagy–lysosome system
proteolysis
signaling
ubiquitin code
ubiquitin-binding domain
ubiquitin–proteasome system
Journal
Trends in biochemical sciences
ISSN: 0968-0004
Titre abrégé: Trends Biochem Sci
Pays: England
ID NLM: 7610674
Informations de publication
Date de publication:
07 2019
07 2019
Historique:
received:
26
11
2018
revised:
23
01
2019
accepted:
29
01
2019
pubmed:
2
3
2019
medline:
18
9
2020
entrez:
2
3
2019
Statut:
ppublish
Résumé
Post-translational modifications (PTMs) by ubiquitin (Ub) are versatile, highly dynamic, and involved in nearly all aspects of eukaryote biological function. The reversibility and heterogeneity of Ub chains attached to protein substrates have complicated their isolation, quantification, and characterization. Strategies have emerged to isolate endogenous ubiquitylated targets, including technologies based on the use of Ub-binding peptides, such as tandem-repeated Ub-binding entities (TUBEs). TUBEs allow the identification and characterization of Ub chains, and novel substrates for deubiquitylases (DUBs) and Ub ligases (E3s). Here we review their impact on purification, analysis of pan or chain-selective polyubiquitylated proteins and underline the biological relevance of this information. Together with peptide aptamers and other Ub affinity-based approaches, TUBEs will contribute to unraveling the secrets of the Ub code.
Identifiants
pubmed: 30819414
pii: S0968-0004(19)30020-9
doi: 10.1016/j.tibs.2019.01.011
pii:
doi:
Substances chimiques
Ubiquitin
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
599-615Informations de copyright
Copyright © 2019 Elsevier Ltd. All rights reserved.