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Interplay between poxviruses and the cellular ubiquitin/ubiquitin-like pathways

期刊

FEBS LETTERS
卷 583, 期 4, 页码 607-614

出版社

WILEY
DOI: 10.1016/j.febslet.2009.01.023

关键词

Ubiquitin; Poxvirus; RING; MARCH; PRANC/F-box; BTB-BACK-Kelch

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Post-translational polypeptide tagging by conjugation with ubiquitin and ubiquitin-like (Ub/Ubl) molecules is a potent way to alter protein functions and/or sort specific protein targets to the proteasome for degradation. Many poxviruses interfere with the host Ub/Ubl system by encoding viral proteins that can usurp this pathway. Some of these include viral proteins of the membrane-associated RING-CH (MARCH) domain, p28/Really Interesting New Gene (RING) finger, ankyrin-repeat/F-box and Broad-complex, Tramtrack and Bric-a-Brac (BTB)/Kelch subgroups of the E3 Ub ligase superfamily. Here we describe and discuss the various strategies used by poxviruses to target and subvert the host cell Ub/Ubl systems. (C) 2009 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

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