Using Ubiquitin Binders to Decipher the Ubiquitin Code.
Trends Biochem Sci
; 44(7): 599-615, 2019 07.
Article
in En
| MEDLINE
| ID: mdl-30819414
ABSTRACT
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.
Key words
Full text:
1
Database:
MEDLINE
Main subject:
Ubiquitin
/
Ubiquitination
Type of study:
Prognostic_studies
Limits:
Animals
/
Humans
Language:
En
Year:
2019
Type:
Article