Poxvirus Exploitation of the Ubiquitin-Proteasome System

被引:33
作者
Barry, Michele [1 ]
van Buuren, Nicholas [1 ]
Burles, Kristin [1 ]
Mottet, Kelly [1 ]
Wang, Qian [1 ]
Teale, Alastair [1 ]
机构
[1] Univ Alberta, Dept Med Microbiol & Immunol, Edmonton, AB T6G 2S2, Canada
来源
VIRUSES-BASEL | 2010年 / 2卷 / 10期
关键词
poxvirus; ubiquitin; F-box; BTB/kelch; RING finger; NF-KAPPA-B; HOST-RANGE PROTEIN; COMPLEX CLASS-I; F-BOX PROTEINS; ANKYRIN-REPEAT PROTEINS; RING FINGER PROTEIN; MYXOMA-VIRUS; ECTROMELIA-VIRUS; MASS-SPECTROMETRY; GENOMIC SEQUENCE;
D O I
10.3390/v2102356
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
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.
引用
收藏
页码:2356 / 2380
页数:25
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