Viral takeover of the host ubiquitin system

Research output: Contribution to journalArticle

31 Citations (Scopus)

Abstract

Like the other more well-characterized post-translational modifications (phosphorylation, methylation, acetylation, acylation, etc.), the attachment of the 76 amino acid ubiquitin (Ub) protein to substrates has been shown to govern countless cellular processes. As obligate intracellular parasites, viruses have evolved the capability to commandeer many host processes in order to maximize their own survival, whether it be to increase viral production or to ensure the long-term survival of latently infected host cells. The first evi-dence that viruses could usurp the Ub system came from the DNA tumor viruses and Adenoviruses, each of which use Ub to dysregulate the host cell cycle (Scheffner et al., 1990; Querido et al., 2001).Today, the list of viruses that utilize Ub includes members from almost every viral class, encompassing both RNA and DNA viruses. Among these, there are examples of Ub usage at every stage of the viral life cycle, involving both ubiquitination and de-ubiquitination. In addition to viruses that merely modify the host Ub system, many of the large DNA viruses encode their own Ub modifying machinery. In this review, we highlight the latest discoveries regarding the myriad ways that viruses utilize Ub to their advantage.

Original languageEnglish (US)
JournalFrontiers in Microbiology
Volume2
Issue numberJULY
DOIs
StatePublished - 2011

Fingerprint

Ubiquitin
Viruses
DNA Viruses
Ubiquitination
DNA Tumor Viruses
Acylation
RNA Viruses
Post Translational Protein Processing
Acetylation
Life Cycle Stages
Adenoviridae
Methylation
Cell Cycle
Parasites
Phosphorylation
Amino Acids

Keywords

  • Proteasome
  • Ubiquitin
  • Ubiquitin ligase complex
  • Ubiquitin proteasome system
  • Viral lifecycle
  • Virus

ASJC Scopus subject areas

  • Microbiology
  • Microbiology (medical)

Cite this

Viral takeover of the host ubiquitin system. / Gustin, Jean; Moses, Ashlee; Frueh, Klaus; Douglas, Janet.

In: Frontiers in Microbiology, Vol. 2, No. JULY, 2011.

Research output: Contribution to journalArticle

@article{01cd39b185d949bb876f76610d4e7136,
title = "Viral takeover of the host ubiquitin system",
abstract = "Like the other more well-characterized post-translational modifications (phosphorylation, methylation, acetylation, acylation, etc.), the attachment of the 76 amino acid ubiquitin (Ub) protein to substrates has been shown to govern countless cellular processes. As obligate intracellular parasites, viruses have evolved the capability to commandeer many host processes in order to maximize their own survival, whether it be to increase viral production or to ensure the long-term survival of latently infected host cells. The first evi-dence that viruses could usurp the Ub system came from the DNA tumor viruses and Adenoviruses, each of which use Ub to dysregulate the host cell cycle (Scheffner et al., 1990; Querido et al., 2001).Today, the list of viruses that utilize Ub includes members from almost every viral class, encompassing both RNA and DNA viruses. Among these, there are examples of Ub usage at every stage of the viral life cycle, involving both ubiquitination and de-ubiquitination. In addition to viruses that merely modify the host Ub system, many of the large DNA viruses encode their own Ub modifying machinery. In this review, we highlight the latest discoveries regarding the myriad ways that viruses utilize Ub to their advantage.",
keywords = "Proteasome, Ubiquitin, Ubiquitin ligase complex, Ubiquitin proteasome system, Viral lifecycle, Virus",
author = "Jean Gustin and Ashlee Moses and Klaus Frueh and Janet Douglas",
year = "2011",
doi = "10.3389/fmicb.2011.00161",
language = "English (US)",
volume = "2",
journal = "Frontiers in Microbiology",
issn = "1664-302X",
publisher = "Frontiers Media S. A.",
number = "JULY",

}

TY - JOUR

T1 - Viral takeover of the host ubiquitin system

AU - Gustin, Jean

AU - Moses, Ashlee

AU - Frueh, Klaus

AU - Douglas, Janet

PY - 2011

Y1 - 2011

N2 - Like the other more well-characterized post-translational modifications (phosphorylation, methylation, acetylation, acylation, etc.), the attachment of the 76 amino acid ubiquitin (Ub) protein to substrates has been shown to govern countless cellular processes. As obligate intracellular parasites, viruses have evolved the capability to commandeer many host processes in order to maximize their own survival, whether it be to increase viral production or to ensure the long-term survival of latently infected host cells. The first evi-dence that viruses could usurp the Ub system came from the DNA tumor viruses and Adenoviruses, each of which use Ub to dysregulate the host cell cycle (Scheffner et al., 1990; Querido et al., 2001).Today, the list of viruses that utilize Ub includes members from almost every viral class, encompassing both RNA and DNA viruses. Among these, there are examples of Ub usage at every stage of the viral life cycle, involving both ubiquitination and de-ubiquitination. In addition to viruses that merely modify the host Ub system, many of the large DNA viruses encode their own Ub modifying machinery. In this review, we highlight the latest discoveries regarding the myriad ways that viruses utilize Ub to their advantage.

AB - Like the other more well-characterized post-translational modifications (phosphorylation, methylation, acetylation, acylation, etc.), the attachment of the 76 amino acid ubiquitin (Ub) protein to substrates has been shown to govern countless cellular processes. As obligate intracellular parasites, viruses have evolved the capability to commandeer many host processes in order to maximize their own survival, whether it be to increase viral production or to ensure the long-term survival of latently infected host cells. The first evi-dence that viruses could usurp the Ub system came from the DNA tumor viruses and Adenoviruses, each of which use Ub to dysregulate the host cell cycle (Scheffner et al., 1990; Querido et al., 2001).Today, the list of viruses that utilize Ub includes members from almost every viral class, encompassing both RNA and DNA viruses. Among these, there are examples of Ub usage at every stage of the viral life cycle, involving both ubiquitination and de-ubiquitination. In addition to viruses that merely modify the host Ub system, many of the large DNA viruses encode their own Ub modifying machinery. In this review, we highlight the latest discoveries regarding the myriad ways that viruses utilize Ub to their advantage.

KW - Proteasome

KW - Ubiquitin

KW - Ubiquitin ligase complex

KW - Ubiquitin proteasome system

KW - Viral lifecycle

KW - Virus

UR - http://www.scopus.com/inward/record.url?scp=84860358241&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84860358241&partnerID=8YFLogxK

U2 - 10.3389/fmicb.2011.00161

DO - 10.3389/fmicb.2011.00161

M3 - Article

C2 - 21847386

AN - SCOPUS:84860358241

VL - 2

JO - Frontiers in Microbiology

JF - Frontiers in Microbiology

SN - 1664-302X

IS - JULY

ER -