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

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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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NF-κB AND REL PROTEINS: Evolutionarily Conserved Mediators of Immune Responses
Ghosh, S., May, M. J., & Kopp, E. B. (1998) · Annual Review of Immunology · doi:10.1146/annurev.immunol.16.1.225 · Cited by 5,182
HOW CELLS RESPOND TO INTERFERONS
Stark, G. R., Kerr, I. M., Williams, B. R. G., Silverman, R. H., & Schreiber, R. D. (1998) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.67.1.227 · Cited by 3,932
Missing Pieces in the NF-κB Puzzle
Ghosh, S., & Karin, M. (2002) · Cell · doi:10.1016/s0092-8674(02)00703-1 · Cited by 3,638
Cytoplasmic Nucleophosmin in Acute Myelogenous Leukemia with a Normal Karyotype
Falini, B., Mecucci, C., Tiacci, E., Alcalay, M., Rosati, R., Pasqualucci, L., La Starza, R., Diverio, D., Colombo, E., Santucci, A., et al. (2005) · New England Journal of Medicine · doi:10.1056/nejmoa041974 · Cited by 1,892
Interferons, interferon‐like cytokines, and their receptors
Pestka, S., Krause, C. D., & Walter, M. R. (2004) · Immunological Reviews · doi:10.1111/j.0105-2896.2004.00204.x · Cited by 1,845
Rel/NF-kappa B/I kappa B family: intimate tales of association and dissociation.Preprint
Verma, I. M., Stevenson, J. K., Schwarz, E. M., Antwerp, D. V., & Miyamoto, S. (1995) · Genes & Development · doi:10.1101/gad.9.22.2723 · Cited by 1,696
Complementation Cloning of NEMO, a Component of the IκB Kinase Complex Essential for NF-κB Activation
Yamaoka, S., Courtois, G., Chable-Bessia, C., Whiteside, S. T., Weil, R., Agou, F., Kirk, H., Kay, R. J., & Israël, A. (1998) · Cell · doi:10.1016/s0092-8674(00)81466-x · Cited by 1,077
TRANSLATIONAL CONTROL IN MAMMALIAN CELLS
Hershey, J. W. B. (1991) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.60.070191.003441 · Cited by 1,029
Molecular cloning and characterization of the human double-stranded RNA-activated protein kinase induced by interferon
MEURS, E. F., Chong, K. L., GALABRU, J., Thomas, N. S. B., Kerr, I. M., Williams, B. R. G., & Hovanessian, A. G. (1990) · Cell · doi:10.1016/0092-8674(90)90374-n · Cited by 1,017
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Mutations in the Nonstructural Protein 5a Gene and Response to Interferon in Patients with Chronic Hepatitis C Virus 1b Infection
Enomoto, N., Sakuma, I., Asahina, Y., Kurosaki, M., Murakami, T., Yamamoto, C., Ogura, Y., Izumi, N., Marumo, F., & Sato, C. (1996) · New England Journal of Medicine · doi:10.1056/nejm199601113340203 · Cited by 997

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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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The dsRNA protein kinase PKR: Virus and cell control

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