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

Leiliang Zhang; Nancy Y. Villa; Grant McFadden

doi:10.1016/j.febslet.2009.01.023

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

Leiliang Zhang, Nancy Y. Villa, Grant McFadden

Research output: Contribution to journal › Short survey › peer-review

40 Scopus citations

Abstract

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.

Original language	English (US)
Pages (from-to)	607-614
Number of pages	8
Journal	FEBS Letters
Volume	583
Issue number	4
DOIs	https://doi.org/10.1016/j.febslet.2009.01.023
State	Published - Feb 18 2009
Externally published	Yes

Keywords

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

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

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10.1016/j.febslet.2009.01.023

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title = "Interplay between poxviruses and the cellular ubiquitin/ubiquitin-like pathways",

abstract = "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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AU - Zhang, Leiliang

AU - Villa, Nancy Y.

AU - McFadden, Grant

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N2 - 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.

AB - 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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KW - MARCH

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KW - Poxvirus

KW - RING

KW - Ubiquitin

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

Abstract

Keywords

ASJC Scopus subject areas

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