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TRIM proteins: another class of viral victims

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TRIM proteins: another class of viral victims. / Munir, Muhammad.
In: Science Signaling, Vol. 3, No. 118, jc2, 20.04.2010.

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Munir M. TRIM proteins: another class of viral victims. Science Signaling. 2010 Apr 20;3(118):jc2. doi: 10.1126/scisignal.3118jc2

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Munir, Muhammad. / TRIM proteins : another class of viral victims. In: Science Signaling. 2010 ; Vol. 3, No. 118.

Bibtex

@article{80b6da67f7a04e0ab033a3129107266c,
title = "TRIM proteins: another class of viral victims",
abstract = "RIM (tripartite motif) proteins are a family of RING (really interesting new gene) domain-containing proteins comprising more than 70 human members, with new members still being described. In addition to their involvement in cell proliferation, differentiation, development, morphogenesis, and apoptosis, roles in immune signaling and antiviral functions are emerging. In response to viral infection, TRIM25 ubiquitinates the N terminus of the viral RNA receptor retinoic acid-inducible gene-I (RIG-I), and this modification is essential for RIG-I to interact with its downstream partner mitochondrial antiviral signaling (MAVS). TRIM25 activity thus leads to activation of the RIG-I signaling pathway, which results in type I interferon production to limit viral replication. Recently, it has been demonstrated that influenza A viruses target TRIM25 and disable its antiviral function, thereby suppressing the host interferon response. This Journal Club article highlights the emerging roles of TRIM proteins in antiviral defense mechanisms and an immune evasion strategy in which influenza viruses target a member of the TRIM family.",
keywords = "DEAD Box Protein 58, DEAD-box RNA Helicases, Humans, Immune Evasion, Immunity, Innate, Interferon Type I, Signal Transduction, Transcription Factors, Tripartite Motif Proteins, Ubiquitin-Protein Ligases, Virus Diseases, Journal Article, Review",
author = "Muhammad Munir",
year = "2010",
month = apr,
day = "20",
doi = "10.1126/scisignal.3118jc2",
language = "English",
volume = "3",
journal = "Science Signaling",
issn = "1945-0877",
publisher = "American Association for the Advancement of Science",
number = "118",

}

RIS

TY - JOUR

T1 - TRIM proteins

T2 - another class of viral victims

AU - Munir, Muhammad

PY - 2010/4/20

Y1 - 2010/4/20

N2 - RIM (tripartite motif) proteins are a family of RING (really interesting new gene) domain-containing proteins comprising more than 70 human members, with new members still being described. In addition to their involvement in cell proliferation, differentiation, development, morphogenesis, and apoptosis, roles in immune signaling and antiviral functions are emerging. In response to viral infection, TRIM25 ubiquitinates the N terminus of the viral RNA receptor retinoic acid-inducible gene-I (RIG-I), and this modification is essential for RIG-I to interact with its downstream partner mitochondrial antiviral signaling (MAVS). TRIM25 activity thus leads to activation of the RIG-I signaling pathway, which results in type I interferon production to limit viral replication. Recently, it has been demonstrated that influenza A viruses target TRIM25 and disable its antiviral function, thereby suppressing the host interferon response. This Journal Club article highlights the emerging roles of TRIM proteins in antiviral defense mechanisms and an immune evasion strategy in which influenza viruses target a member of the TRIM family.

AB - RIM (tripartite motif) proteins are a family of RING (really interesting new gene) domain-containing proteins comprising more than 70 human members, with new members still being described. In addition to their involvement in cell proliferation, differentiation, development, morphogenesis, and apoptosis, roles in immune signaling and antiviral functions are emerging. In response to viral infection, TRIM25 ubiquitinates the N terminus of the viral RNA receptor retinoic acid-inducible gene-I (RIG-I), and this modification is essential for RIG-I to interact with its downstream partner mitochondrial antiviral signaling (MAVS). TRIM25 activity thus leads to activation of the RIG-I signaling pathway, which results in type I interferon production to limit viral replication. Recently, it has been demonstrated that influenza A viruses target TRIM25 and disable its antiviral function, thereby suppressing the host interferon response. This Journal Club article highlights the emerging roles of TRIM proteins in antiviral defense mechanisms and an immune evasion strategy in which influenza viruses target a member of the TRIM family.

KW - DEAD Box Protein 58

KW - DEAD-box RNA Helicases

KW - Humans

KW - Immune Evasion

KW - Immunity, Innate

KW - Interferon Type I

KW - Signal Transduction

KW - Transcription Factors

KW - Tripartite Motif Proteins

KW - Ubiquitin-Protein Ligases

KW - Virus Diseases

KW - Journal Article

KW - Review

U2 - 10.1126/scisignal.3118jc2

DO - 10.1126/scisignal.3118jc2

M3 - Journal article

C2 - 20407122

VL - 3

JO - Science Signaling

JF - Science Signaling

SN - 1945-0877

IS - 118

M1 - jc2

ER -