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  5. Ubiquitin chain specific auto-ubiquitination triggers sustained oscillation, bistable switches and excitable firing
 
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Ubiquitin chain specific auto-ubiquitination triggers sustained oscillation, bistable switches and excitable firing

Author(s)
Nguyen, Lan K.  
Zhao, Qi  
Varusai, Thawfeek M.  
Kholodenko, Boris N.  
Uri
http://hdl.handle.net/10197/9788
Date Issued
2014-12
Date Available
2019-04-03T09:46:23Z
Abstract
Ubiquitin modification of cellular proteins commonly targets them for proteosomal degradation, but can also convey non-proteolytic functions. Over the past years, advances in experimental approaches have helped uncover the extensive involvement of ubiquitination in protein regulation. However, our understanding of the dynamics of the ubiquitination-related networks have lagged behind. A common regulatory theme for many E3 ligases is the ability to self-catalyse their own ubiquitination without involving external E3 ligating enzymes. Here, the authors have explored computational models of both proteolytic and non-proteolytic auto-ubiquitination of E3 ligases and characterised the dynamic properties of these regulatory motifs. Remarkably, in both cases auto-ubiquitination coupled with multi-step de-ubiquitination process can bring about sustained oscillatory behaviour. In addition, the same basic wiring structures can trigger bistable switches of activity and excitable firing of the dynamic responses of the ubiquitinated E3 ligase. Bifurcation analysis allows one to derive parametric conditions that govern these dynamics. They also show that these complex non-linear behaviours persist for a more detailed mechanistic description that involves the E1 and E2 enzymes. Their work therefore provides new insights into the dynamic features of auto-ubiquitination in different cellular contexts.
Sponsorship
European Commission - Seventh Framework Programme (FP7)
Science Foundation Ireland
Other Sponsorship
UCD Seed Funding program
National Natural Science Foundation of China
Type of Material
Journal Article
Publisher
Institution of Engineering and Technology
Volume
8
Issue
6
Start Page
282
End Page
292
Copyright (Published Version)
2015 the Authors
Subjects

Ubiquitin

Protein degradation

Protein trafficking

Cell cycle progressio...

Ubiquitin molecule

Auto-ubiquitination

DOI
10.1049/iet-syb.2014.0024
Language
English
Status of Item
Peer reviewed
This item is made available under a Creative Commons License
https://creativecommons.org/licenses/by-nc-nd/3.0/ie/
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Ubiquitin chain specific auto-ubiquitination triggers...pdf

Size

1.1 MB

Format

Adobe PDF

Checksum (MD5)

049a07c795135c2b231e512719f5483f

Owning collection
SBI Research Collection
Mapped collections
Conway Institute Research Collection•
Medicine Research Collection

Item descriptive metadata is released under a CC-0 (public domain) license: https://creativecommons.org/public-domain/cc0/.
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