https://www.annualreviews.org/doi/abs/10.1146/annurev-biochem-061516-044916?journalCode=biochem
Mechanisms of Deubiquitinase Specificity and Regulation
Annual Review of Biochemistry
Vol. 86:159-192 (Volume publication date June 2017)
First published as a Review in Advance on May 12, 2017
https://doi.org/10.1146/annurev-biochem-061516-044916 Abstract
Protein
ubiquitination is one of the most powerful posttranslational
modifications of proteins, as it regulates a plethora of cellular
processes in distinct manners. Simple monoubiquitination events coexist
with more complex forms of polyubiquitination, the latter featuring many
different chain architectures. Ubiquitin can be subjected to further
posttranslational modifications (e.g., phosphorylation and acetylation)
and can also be part of mixed polymers with ubiquitin-like modifiers
such as SUMO (small ubiquitin-related modifier) or NEDD8 (neural
precursor cell expressed, developmentally downregulated 8). Together,
cellular ubiquitination events form a sophisticated and versatile
ubiquitin code.
Deubiquitinases (DUBs) reverse ubiquitin signals with equally high sophistication. In this review, we conceptualize the many layers of specificity that DUBs encompass to control the ubiquitin code and discuss examples in which DUB specificity has been understood at the molecular level. We further discuss the many mechanisms of DUB regulation with a focus on those that modulate catalytic activity. Our review provides a framework to tackle lingering questions in DUB biology.
USP-DUBs
http://flybase.org/reports/FBgg0000170.html
Deubiquitinases (DUBs) reverse ubiquitin signals with equally high sophistication. In this review, we conceptualize the many layers of specificity that DUBs encompass to control the ubiquitin code and discuss examples in which DUB specificity has been understood at the molecular level. We further discuss the many mechanisms of DUB regulation with a focus on those that modulate catalytic activity. Our review provides a framework to tackle lingering questions in DUB biology.
- 5 groups
Deubiquitinases
(DUBs) catalyze the proteolytic removal of ubiquitin from ubiquitin
chains and ubiquinated proteins. DUBs can be divided into five
sub-families:
- ubiquitin C-terminal hydrolases (UCHs),
- ubiquitin-specific proteases (USPs),
- ovarian tumour proteases (OTUs),
- Josephins and
- JAB1/MPN/MOV34 metalloenzymes (JAMMs).
(Adapted from PMID:19626045).
USP-DUBs
http://flybase.org/reports/FBgg0000170.html
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