Poxvirus Exploitation of the Ubiquitin-Proteasome System 英文参考文献.docVIP

Viruses 2010, 2, 2356-2380; doi:10.3390/v2102356 OPEN ACCESS viruses ISSN 1999-4915 /journal/viruses Review Poxvirus Exploitation of the Ubiquitin-Proteasome System Michele Barry *, Nicholas van Buuren, Kristin Burles, Kelly Mottet, Qian Wang and Alastair Teale Department of Medical Microbiology and Immunology, University of Alberta, Edmonton, T6G 2S2, Canada; E-Mails: njv@ualberta.ca (N.v.B.); burles@ualberta.ca (K.B.); kmottet@ualberta.ca (K.M.); qw1@ualberta.ca (Q.W.); ateale@ualberta.ca (A.T.) * Author to whom correspondence should be addressed: E-Mail: michele.barry@ualberta.ca; Tel.: +1 780 492-0702; Fax: +1 780 492-7521. 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 finger 1. Introduction Ubiquitin is a 76 amino acid protein that is best known for its role in protein degradation [1], however, the addition of ubiquitin can also serve roles not associated with protein degradation [2]. The post-translational addition of ubiquitin onto proteins occurs through a three step enzymatic cascade [3]. Ubiquitin is initially activated by one of two ubiquitin activating enzymes. Activated ubiquitin is subsequently transferred to a ubiquitin conjugating enzyme.