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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Detalles Bibliográficos
Autores principales: Barry, Michele, van Buuren, Nicholas, Burles, Kristin, Mottet, Kelly, Wang, Qian, Teale, Alastair
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Molecular Diversity Preservation International (MDPI) 2010
Materias:
Review
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3185573/
https://www.ncbi.nlm.nih.gov/pubmed/21994622
http://dx.doi.org/10.3390/v2102356
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author Barry, Michele
van Buuren, Nicholas
Burles, Kristin
Mottet, Kelly
Wang, Qian
Teale, Alastair
author_facet Barry, Michele
van Buuren, Nicholas
Burles, Kristin
Mottet, Kelly
Wang, Qian
Teale, Alastair
author_sort Barry, Michele
collection PubMed
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.
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spelling pubmed-31855732011-10-12 Poxvirus Exploitation of the Ubiquitin-Proteasome System Barry, Michele van Buuren, Nicholas Burles, Kristin Mottet, Kelly Wang, Qian Teale, Alastair Viruses Review 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. Molecular Diversity Preservation International (MDPI) 2010-10-19 /pmc/articles/PMC3185573/ /pubmed/21994622 http://dx.doi.org/10.3390/v2102356 Text en © 2010 by the authors; licensee MDPI, Basel, Switzerland. http://creativecommons.org/licenses/by/3.0 This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/).
spellingShingle Review
Barry, Michele
van Buuren, Nicholas
Burles, Kristin
Mottet, Kelly
Wang, Qian
Teale, Alastair
Poxvirus Exploitation of the Ubiquitin-Proteasome System
title Poxvirus Exploitation of the Ubiquitin-Proteasome System
title_full Poxvirus Exploitation of the Ubiquitin-Proteasome System
title_fullStr Poxvirus Exploitation of the Ubiquitin-Proteasome System
title_full_unstemmed Poxvirus Exploitation of the Ubiquitin-Proteasome System
title_short Poxvirus Exploitation of the Ubiquitin-Proteasome System
title_sort poxvirus exploitation of the ubiquitin-proteasome system
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3185573/
https://www.ncbi.nlm.nih.gov/pubmed/21994622
http://dx.doi.org/10.3390/v2102356
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