Poxvirus exploitation of the ubiquitin-proteasome system

Ubiquitination plays a critical role in many cellular processes. A growing number of viruses have evolved strategies to exploit the ubiquitin-proteasome system, including members of the Poxviridae family. Members of the poxvirus family have recently been shown to encode BTB/kelch and ankyrin/F-box p...

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Published in:Viruses 2010-10, Vol.2 (10), p.2356-2380
Main Authors: Barry, Michele, van Buuren, Nicholas, Burles, Kristin, Mottet, Kelly, Wang, Qian, Teale, Alastair
Format: Article
Language:English
Subjects:
BTB/kelch
F-box
Poxviridae
Poxvirus
Review
RING finge
ubiquitin
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description Ubiquitination plays a critical role in many cellular processes. A growing number of viruses have evolved strategies to exploit the ubiquitin-proteasome system, including members of the Poxviridae family. Members of the poxvirus family have recently been shown to encode BTB/kelch and ankyrin/F-box proteins that interact with cullin-3 and cullin-1 based ubiquitin ligases, respectively. Multiple members of the poxvirus family also encode ubiquitin ligases with intrinsic activity. This review describes the numerous mechanisms that poxviruses employ to manipulate the ubiquitin-proteasome system.
doi_str_mv 10.3390/v2102356
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1999-4915
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subjects BTB/kelch
F-box
Poxviridae
Poxvirus
Review
RING finge
ubiquitin
title Poxvirus exploitation of the ubiquitin-proteasome system
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