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Interplay between poxviruses and the cellular ubiquitin/ubiquitin‐like pathways
Author(s) -
Zhang Leiliang,
Villa Nancy Y.,
McFadden Grant
Publication year - 2009
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2009.01.023
Subject(s) - ubiquitin , ubiquitin ligase , proteasome , nedd4 , microbiology and biotechnology , ring finger , biology , deubiquitinating enzyme , ankyrin , ubiquitin protein ligases , ubiquitins , ankyrin repeat , escrt , ring finger domain , genetics , zinc finger , gene , endosome , transcription factor , intracellular
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.