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Cited by 645interferon and immune responsesEndoplasmic Reticulum Stress and DiseaseRNA and protein synthesis mechanisms

The DOI matches its Crossref record; 207 of the 210 references it cites were found in a registry or an index.

The dsRNA protein kinase PKR: Virus and cell control

García, M.A., Meurs, E.F., Esteban, M.·2007·Biochimie
DOI 10.1016/j.biochi.2007.03.001
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Abstract

The IFN-induced double-stranded RNA-dependent protein kinase (PKR) is one of the four mammalian serine-threonine kinases (the three others being HRI, GCN2 and PERK) that phosphorylate the eIF2 alpha translation initiation factor, in response to stress signals, mainly as a result of viral infections. eIF2 alpha phosphorylation results in arrest of translation of both cellular and viral mRNAs, an efficient way to inhibit virus replication. The particularity of PKR is to activate by binding to dsRNA through two N terminal dsRNA binding motifs (dsRBM). PKR activation during a viral infection represents a threat for several viruses, which have therefore evolved to express PKR inhibitors, such as the Vaccinia E3L and K3L proteins. The function of PKR can also be regulated by cellular proteins, either positively (RAX/PACT; Mda7) or negatively (p58IPK, TRBP, nucleophosmin, Hsp90/70). PKR can provoke apoptosis, in part through its ability to control protein translation, but the situation appears to be more complex, as NF-kappaB, ATF-3 and p53 have also been implicated. PKR-induced apoptosis involves mainly the FADD/caspase 8 pathway, while the mitochondrial APAF/caspase 9 pathway is also engaged. As a consequence of the effects of PKR on translation, transcription and apoptosis, PKR can function to control cell growth and cell differentiation, and its activity can be controlled by the action of several oncogenes.

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Metadata

Authors
García, M. A., Meurs, E. F., & Esteban, M.
Affiliations
Institut Pasteur (FR)
ORCID
Meurs, E.F.
Venue
Biochimie
Publisher
Elsevier BV
Published
2007-06
Volume
89
Issue
6-7
Pages
799-811
ISSN
  • 0037-9042 (ISSN-L)
  • 0300-9084
DOI
10.1016/j.biochi.2007.03.001
OpenAlex
W2085487477
Cited by
644
References
210
Citations by year
2026: 16 · 2025: 30 · 2024: 32 · 2023: 38 · 2022: 33 · 2021: 44 · 2020: 49 · 2019: 20 · 2018: 24 · 2017: 25 · 2016: 25 · 2015: 30 · 2014: 34 · 2013: 38 · 2012: 58
FWCI
2.91
Type
journal article
Language
en
Open access
closed
Licence
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations
  • Biochimie (publishedVersion)
  • PubMed (publishedVersion)
Topics
  • Life Sciences › Immunology and Microbiology › Immunology › interferon and immune responses
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Endoplasmic Reticulum Stress and Disease
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
Keywords
PKR, double-stranded RNA-dependent protein kinase, eIF2α phosphorylation, translational arrest, antiviral innate immunity, interferon signaling, PKR inhibitor, p58IPK, TRBP, nucleophosmin, apoptosis, NF-κB, ATF3, p53, oncogenes, cell growth and differentiation, viral replication inhibition
MeSH terms
Animals, Antiviral Agents, Gene Expression Regulation, Humans, Models, Biological, RNA, Messenger, Protein Biosynthesis, Signal Transduction, Gene Expression Regulation, Viral, NF-kappa B, Apoptosis, Protein Structure, Tertiary, eIF-2 Kinase, Amino Acid Motifs, Cell Proliferation

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