TRIMmunity

The roles of the TRIM E3-ubiquitin ligase family in innate antiviral immunity

Ricardo Rajsbaum Gorodezky, Adolfo García-Sastre, Gijs A. Versteeg

Research output: Contribution to journalArticle

126 Citations (Scopus)

Abstract

Tripartite motif (TRIM) proteins have been implicated in multiple cellular functions, including antiviral activity. Research efforts so far indicate that the antiviral activity of TRIMs relies, for the most part, on their function as E3-ubiquitin ligases. A substantial number of the TRIM family members have been demonstrated to mediate innate immune cell signal transduction and subsequent cytokine induction. In addition, a subset of TRIMs has been shown to restrict viral replication by directly targeting viral proteins. Although the body of work on the cellular roles of TRIM E3-ubiquitin ligases has rapidly grown over the last years, many aspects of their molecular workings and multi-functionality remain unclear. The antiviral function of many TRIMs seems to be conferred by specific isoforms, by sub-cellular localization and in cell-type-specific contexts. Here we review recent findings on TRIM antiviral functions, current limitations and an outlook for future research.

Original languageEnglish (US)
Pages (from-to)1265-1284
Number of pages20
JournalJournal of Molecular Biology
Volume426
Issue number6
DOIs
StatePublished - Mar 20 2014
Externally publishedYes

Fingerprint

Ubiquitin-Protein Ligases
Innate Immunity
Antiviral Agents
Viral Proteins
Signal Transduction
Protein Isoforms
Cytokines
Research

Keywords

  • antiviral response
  • E3-ubiquitin ligase
  • innate immunity
  • restriction factors
  • tripartite motif

ASJC Scopus subject areas

  • Molecular Biology

Cite this

TRIMmunity : The roles of the TRIM E3-ubiquitin ligase family in innate antiviral immunity. / Rajsbaum Gorodezky, Ricardo; García-Sastre, Adolfo; Versteeg, Gijs A.

In: Journal of Molecular Biology, Vol. 426, No. 6, 20.03.2014, p. 1265-1284.

Research output: Contribution to journalArticle

@article{0dca49c16c9c4e308570c007dc776122,
title = "TRIMmunity: The roles of the TRIM E3-ubiquitin ligase family in innate antiviral immunity",
abstract = "Tripartite motif (TRIM) proteins have been implicated in multiple cellular functions, including antiviral activity. Research efforts so far indicate that the antiviral activity of TRIMs relies, for the most part, on their function as E3-ubiquitin ligases. A substantial number of the TRIM family members have been demonstrated to mediate innate immune cell signal transduction and subsequent cytokine induction. In addition, a subset of TRIMs has been shown to restrict viral replication by directly targeting viral proteins. Although the body of work on the cellular roles of TRIM E3-ubiquitin ligases has rapidly grown over the last years, many aspects of their molecular workings and multi-functionality remain unclear. The antiviral function of many TRIMs seems to be conferred by specific isoforms, by sub-cellular localization and in cell-type-specific contexts. Here we review recent findings on TRIM antiviral functions, current limitations and an outlook for future research.",
keywords = "antiviral response, E3-ubiquitin ligase, innate immunity, restriction factors, tripartite motif",
author = "{Rajsbaum Gorodezky}, Ricardo and Adolfo Garc{\'i}a-Sastre and Versteeg, {Gijs A.}",
year = "2014",
month = "3",
day = "20",
doi = "10.1016/j.jmb.2013.12.005",
language = "English (US)",
volume = "426",
pages = "1265--1284",
journal = "Journal of Molecular Biology",
issn = "0022-2836",
publisher = "Academic Press Inc.",
number = "6",

}

TY - JOUR

T1 - TRIMmunity

T2 - The roles of the TRIM E3-ubiquitin ligase family in innate antiviral immunity

AU - Rajsbaum Gorodezky, Ricardo

AU - García-Sastre, Adolfo

AU - Versteeg, Gijs A.

PY - 2014/3/20

Y1 - 2014/3/20

N2 - Tripartite motif (TRIM) proteins have been implicated in multiple cellular functions, including antiviral activity. Research efforts so far indicate that the antiviral activity of TRIMs relies, for the most part, on their function as E3-ubiquitin ligases. A substantial number of the TRIM family members have been demonstrated to mediate innate immune cell signal transduction and subsequent cytokine induction. In addition, a subset of TRIMs has been shown to restrict viral replication by directly targeting viral proteins. Although the body of work on the cellular roles of TRIM E3-ubiquitin ligases has rapidly grown over the last years, many aspects of their molecular workings and multi-functionality remain unclear. The antiviral function of many TRIMs seems to be conferred by specific isoforms, by sub-cellular localization and in cell-type-specific contexts. Here we review recent findings on TRIM antiviral functions, current limitations and an outlook for future research.

AB - Tripartite motif (TRIM) proteins have been implicated in multiple cellular functions, including antiviral activity. Research efforts so far indicate that the antiviral activity of TRIMs relies, for the most part, on their function as E3-ubiquitin ligases. A substantial number of the TRIM family members have been demonstrated to mediate innate immune cell signal transduction and subsequent cytokine induction. In addition, a subset of TRIMs has been shown to restrict viral replication by directly targeting viral proteins. Although the body of work on the cellular roles of TRIM E3-ubiquitin ligases has rapidly grown over the last years, many aspects of their molecular workings and multi-functionality remain unclear. The antiviral function of many TRIMs seems to be conferred by specific isoforms, by sub-cellular localization and in cell-type-specific contexts. Here we review recent findings on TRIM antiviral functions, current limitations and an outlook for future research.

KW - antiviral response

KW - E3-ubiquitin ligase

KW - innate immunity

KW - restriction factors

KW - tripartite motif

UR - http://www.scopus.com/inward/record.url?scp=84894515095&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84894515095&partnerID=8YFLogxK

U2 - 10.1016/j.jmb.2013.12.005

DO - 10.1016/j.jmb.2013.12.005

M3 - Article

VL - 426

SP - 1265

EP - 1284

JO - Journal of Molecular Biology

JF - Journal of Molecular Biology

SN - 0022-2836

IS - 6

ER -