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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.
Received: 2 September 2010; in revised form: 27 September 2010 / Accepted: 30 September 2010 / Published: 19 October 2010
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
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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.
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.
Barry, Michele; Van Buuren, Nicholas; Burles, Kristin; Mottet, Kelly; Wang, Qian; Teale, Alastair. 2010. "Poxvirus Exploitation of the Ubiquitin-Proteasome System." Viruses 2, no. 10: 2356-2380.