Interplay between poxviruses and the cellular ubiquitin/ubiquitin‐like pathways | Zendy

Zhang Leiliang | Zendy; Villa Nancy Y. | Zendy; McFadden Grant | Zendy

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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.

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