Biotin-Based Strategies to Explore the World of Ubiquitin and Ubiquitin-Like Modifiers.
Biotin
E3 ligase
Proximity proteomics
SUMO
Ubiquitin
Journal
Chembiochem : a European journal of chemical biology
ISSN: 1439-7633
Titre abrégé: Chembiochem
Pays: Germany
ID NLM: 100937360
Informations de publication
Date de publication:
15 Mar 2024
15 Mar 2024
Historique:
revised:
07
12
2023
received:
31
10
2023
medline:
18
3
2024
pubmed:
12
12
2023
entrez:
11
12
2023
Statut:
ppublish
Résumé
A complex code of cellular signals is mediated by ubiquitin and ubiquitin-like (Ub/UbL) modifications on substrate proteins. The so-called Ubiquitin Code specifies protein fates, such as stability, subcellular localization, functional activation or suppression, and interactions. Hundreds of enzymes are involved in placing and removing Ub/UbL on thousands of substrates, while the consequences of modifications and the mechanisms of specificity are still poorly defined. Challenges include rapid and transient engagement of enzymes and Ub/UbL interactors, low stoichiometry of modified versus non-modified cellular substrates, and protease-mediated loss of Ub/UbL in lysates. To decipher this complexity and confront the challenges, many tools have been created to trap and identify substrates and interactors linked to Ub/UbL modification. This review focuses on an assortment of biotin-based tools developed for this purpose (for example BioUbLs, UbL-ID, BioE3, BioID), taking advantage of the strong affinity of biotin-streptavidin and the stringent lysis/washing approach allowed by it, paired with sensitive mass-spectrometry-based proteomic methods. Knowing how substrates change during development and disease, the consequences of substrate modification, and matching substrates to particular UbL-ligating enzymes will contribute new insights into how Ub/UbL signaling works and how it can be exploited for therapies.
Identifiants
pubmed: 38081789
doi: 10.1002/cbic.202300746
doi:
Substances chimiques
Ubiquitin
0
Biotin
6SO6U10H04
Peptide Hydrolases
EC 3.4.-
Types de publication
Review
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
e202300746Subventions
Organisme : MCIN/AEI/10.13039/501100011033
ID : PID2020-114178GB-I00
Organisme : MCIN/AEI/10.13039/501100011033
ID : CEX2021-001136-S
Organisme : Department of Industry, Tourism, and Trade of the Basque Country Government
Organisme : Innovation Technology Department of the Bizkaia County
ID : 765445-EU
Organisme : European Cooperation for Science & Technology ProteoCure COST Action
ID : CA20113
Organisme : FPU
ID : FPU20/05282
Organisme : Ministerio de Universidades para la Formación de Profesorado Universitario
Organisme : Spanish MCIU
ID : PID2020-117333GB-I00
Informations de copyright
© 2023 Wiley-VCH GmbH.
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