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MDPI, Viruses, 10(2), p. 2356-2380, 2010

DOI: 10.3390/v2102356

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Poxvirus Exploitation of the Ubiquitin-Proteasome System

Journal article published in 2010 by Michele Barry, Nicholas van Buuren ORCID, Kristin Burles, Kelly Mottet, Qian Wang, Alastair Teale
This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

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Abstract

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.