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Review

Poxvirus Exploitation of the Ubiquitin-Proteasome System

Department of Medical Microbiology and Immunology, University of Alberta, Edmonton, T6G 2S2, Canada
*
Author to whom correspondence should be addressed.
Viruses 2010, 2(10), 2356-2380; https://doi.org/10.3390/v2102356
Submission received: 2 September 2010 / Revised: 27 September 2010 / Accepted: 30 September 2010 / Published: 19 October 2010
(This article belongs to the Special Issue Viruses and the Ubiquitin/Proteasome System)

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.
Keywords: poxvirus; ubiquitin; F-box; BTB/kelch; RING finge poxvirus; ubiquitin; F-box; BTB/kelch; RING finge

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MDPI and ACS Style

Barry, M.; Van Buuren, N.; Burles, K.; Mottet, K.; Wang, Q.; Teale, A. Poxvirus Exploitation of the Ubiquitin-Proteasome System. Viruses 2010, 2, 2356-2380. https://doi.org/10.3390/v2102356

AMA Style

Barry M, Van Buuren N, Burles K, Mottet K, Wang Q, Teale A. Poxvirus Exploitation of the Ubiquitin-Proteasome System. Viruses. 2010; 2(10):2356-2380. https://doi.org/10.3390/v2102356

Chicago/Turabian Style

Barry, Michele, Nicholas Van Buuren, Kristin Burles, Kelly Mottet, Qian Wang, and Alastair Teale. 2010. "Poxvirus Exploitation of the Ubiquitin-Proteasome System" Viruses 2, no. 10: 2356-2380. https://doi.org/10.3390/v2102356

APA Style

Barry, M., Van Buuren, N., Burles, K., Mottet, K., Wang, Q., & Teale, A. (2010). Poxvirus Exploitation of the Ubiquitin-Proteasome System. Viruses, 2(10), 2356-2380. https://doi.org/10.3390/v2102356

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