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

Leiliang Zhang, Nancy Villa, Douglas McFadden

Research output: Contribution to journalShort survey

30 Citations (Scopus)

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 languageEnglish (US)
Pages (from-to)607-614
Number of pages8
JournalFEBS Letters
Volume583
Issue number4
DOIs
StatePublished - Feb 18 2009
Externally publishedYes

Fingerprint

Poxviridae
Ubiquitin
Viral Matrix Proteins
Genes
Ankyrin Repeat
Ubiquitin-Protein Ligases
Viral Proteins
Proteasome Endopeptidase Complex
Ligases
Fingers
Proteins
Degradation
Peptides
Molecules

Keywords

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

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

Cite this

Interplay between poxviruses and the cellular ubiquitin/ubiquitin-like pathways. / Zhang, Leiliang; Villa, Nancy; McFadden, Douglas.

In: FEBS Letters, Vol. 583, No. 4, 18.02.2009, p. 607-614.

Research output: Contribution to journalShort survey

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