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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Comparative analysis of the regulation of the interferoninducible protein kinase PKR by Epstein - Barr virus RNAs EBER-1 and EBER-2 and adenovirus VA, RNA
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Mechanism of Interferon Action: Inhibition of Viral Messenger Ribonucleic Acid Translation in L-Cell Extracts
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Protein Synthesis and Endoplasmic Reticulum Stress Can Be Modulated by the Hepatitis C Virus Envelope Protein E2 through the Eukaryotic Initiation Factor 2α Kinase PERK
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HIV-1 Tat Directly Interacts with the Interferon-Induced, Double-Stranded RNA-Dependent Kinase, PKR
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The binding of double‐stranded RNA and adenovirus VAI RNA to the interferon‐induced protein kinase
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TRAF Family Proteins Link PKR with NF-κB Activation
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Double-Stranded-RNA-Activated Protein Kinase PKR Enhances Transcriptional Activation by Tumor Suppressor p53
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Double-stranded RNA-dependent Protein Kinase Phosphorylation of the α-Subunit of Eukaryotic Translation Initiation Factor 2 Mediates Apoptosis
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Sequence analysis of the NS5A protein of European hepatitis C virus 1b isolates and relation to interferon sensitivity.
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Adenoviral transfer of the melanoma differentiation-associated gene 7 (mda7) induces apoptosis of lung cancer cells via up-regulation of the double-stranded RNA-dependent protein kinase (PKR).
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The Hsp90 chaperone complex is both a facilitator and a repressor of the dsRNA‐dependent kinase PKR
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The Apoptosis Pathway Triggered by the Interferon-Induced Protein Kinase PKR Requires the Third Basic Domain, Initiates Upstream of Bcl-2, and Involves ICE-like Proteases1
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The Vaccinia Virus E3L Gene Product Interacts with both the Regulatory and the Substrate Binding Regions of PKR: Implications for PKR Autoregulation
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The 58-kilodalton inhibitor of the interferon-induced double-stranded RNA-activated protein kinase is a tetratricopeptide repeat protein with oncogenic properties.
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Inhibition of PACT-Mediated Activation of PKR by the Herpes Simplex Virus Type 1 Us11 Protein
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Nuclear Localization of the Interferon-Inducible Protein Kinase PKR in Human Cells and Transfected Mouse Cells
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The Herpes Simplex Virus Type 1 U S 11 Protein Interacts with Protein Kinase R in Infected Cells and Requires a 30-Amino-Acid Sequence Adjacent to a Kinase Substrate Domain
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Distinct Patterns of IFN Sensitivity Observed in Cells Infected with Vaccinia K3L- and E3L- Mutant Viruses
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IRF-1 induced cell growth inhibition and interferon induction requires the activity of the protein kinase PKR.
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The protein kinase PKR: a molecular clock that sequentially activates survival and death programs
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Higher-Order Substrate Recognition of eIF2α by the RNA-Dependent Protein Kinase PKR
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The Anti-apoptotic Function of Hsp70 in the Interferon-inducible Double-stranded RNA-dependent Protein Kinase-mediated Death Signaling Pathway Requires the Fanconi Anemia Protein, FANCC
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Human breast cancer cells contain elevated levels and activity of the protein kinase, PKR
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Double-Stranded RNA-Dependent Protein Kinase (PKR) Is Regulated by Reovirus Structural Proteins
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Two Dimerization Domains in the Trans-activation Response RNA-binding Protein (TRBP) Individually Reverse the Protein Kinase R Inhibition of HIV-1 Long Terminal Repeat Expression
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Control of α Subunit of Eukaryotic Translation Initiation Factor 2 (eIF2α) Phosphorylation by the Human Papillomavirus Type 18 E6 Oncoprotein: Implications for eIF2α-Dependent Gene Expression and Cell Death
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Interaction of influenza virus NS1 protein and the human homologue of Staufen in vivo and in vitro
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Detection of a Novel Unglycosylated Form of Hepatitis C Virus E2 Envelope Protein That Is Located in the Cytosol and Interacts with PKR
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Neoplastic progression in melanoma and colon cancer is associated with increased expression and activity of the interferon-inducible protein kinase, PKR
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Double-Stranded RNA-Activated Protein Kinase (PKR) Is Negatively Regulated by 60S Ribosomal Subunit Protein L18
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Low TRBP Levels Support an Innate Human Immunodeficiency Virus Type 1 Resistance in Astrocytes by Enhancing the PKR Antiviral Response
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Folding and dimerization of hepatitis C virus E1 and E2 glycoproteins in stably transfected CHO cells
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Protein kinase PKR is required for platelet‐derived growth factor signaling of c‐fos gene expression via Erks and Stat3
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Ribosome Targeting of PKR Is Mediated by Two Double-stranded RNA-binding Domains and Facilitates in Vivo Phosphorylation of Eukaryotic Initiation Factor-2
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Molecular Mechanisms Responsible for Malignant Transformation by Regulatory and Catalytic Domain Variants of the Interferon-induced Enzyme RNA-dependent Protein Kinase
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Tyrosine phosphorylation acts as a molecular switch to full-scale activation of the eIF2α RNA-dependent protein kinase
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The latency protein LANA2 from Kaposi's sarcoma-associated herpesvirus inhibits apoptosis induced by dsRNA-activated protein kinase but not RNase L activation
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Inhibitory role of the host apoptogenic gene PKR in the establishment of persistent infection by encephalomyocarditis virus in U937 cells
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Functional Characterization of pkr Gene Products Expressed in Cells from Mice with a Targeted Deletion of the N terminus or C terminus Domain of PKR
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Evidence that avian reovirus σA protein is an inhibitor of the double-stranded RNA-dependent protein kinase
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The catalytic activity of dsRNA-dependent protein kinase, PKR, is required for NF-κB activation
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The N-terminus of PKR is responsible for the activation of the NF-κB signaling pathway by interacting with the IKK complex
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Complementation of Vaccinia Virus Deleted of the E3L Gene by Mutants of E3L
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Activation of the interferon-inducible protein kinase PKR by Hepatocellular carcinoma derived-Hepatitis C virus core protein
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Cell cycle regulation of the double stranded RNA activated protein kinase, PKR
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Protection from Interferon-Induced Apoptosis by Epstein-Barr Virus Small RNAs Is Not Mediated by Inhibition of PKR
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Double-stranded RNA-dependent Protein Kinase Mediates c-Myc Suppression Induced by Type I Interferons
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Expression of the protein kinase PKR in modulated by IRF-1 and is reduced in 5q- associated leukemias.
Beretta, L., Gabbay, M., Berger, R., Hanash, S., & Sonenberg, N. (1996) · PubMed · Cited by 68
Melanoma differentiation-associated gene-7 protein physically associates with the double-stranded RNA-activated protein kinase PKR
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Tat-responsive region RNA of human immunodeficiency virus type 1 stimulates protein synthesis in vivo and in vitro: relationship between structure and function.
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Phosphorylation of HIV Tat by PKR increases interaction with TAR RNA and enhances transcription
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Serine 18 Phosphorylation of RAX, the PKR Activator, Is Required for PKR Activation and Consequent Translation Inhibition
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Identification of a Lytic-Cycle Epstein-Barr Virus Gene Product That Can Regulate PKR Activation
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The Interferon-Induced Double-Stranded RNA-Activated Human p68 Protein Kinase Potently Inhibits Protein Synthesis in Cultured Cells
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Further characterization of the protein kinase activity mediated by interferon in mouse and human cells.
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Caspase 9 activation by the dsRNA‐dependent protein kinase, PKR: molecular mechanism and relevance
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Nucleophosmin Interacts with and Inhibits the Catalytic Function of Eukaryotic Initiation Factor 2 Kinase PKR
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Antiviral action of the tumor suppressor ARF
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Anti-apoptotic and oncogenic properties of the dsRNA-binding protein of vaccinia virus, E3L
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Specific Recognition of HIV TAR RNA by the dsRNA Binding Domains (dsRBD1–dsRBD2) of PKR
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Regulation of GTP hydrolysis prior to ribosomal AUG selection during eukaryotic translation initiation
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Endogenous inhibitors of the dsRNA-dependent eIF-2α protein kinase PKR in normal and ras-transformed cells
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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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