ArticleOncogene2001
The catalytic activity of dsRNA-dependent protein kinase, PKR, is required for NF-kappaB activation.
Article in Oncogene, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed, 71 citations in OpenAlex.
- PACT suppresses PKR activation through dsRNA binding and dimerization, and is a therapeutic target for triple-negative breast cancer.RNA (New York, N.Y.) · 2025Article
- Roles and Applications of Circular RNA in Virus Infection.International journal of molecular sciences · 2025Review
- Poxvirus K3 Orthologs Regulate NF-κB-Dependent Inflammatory Responses by Targeting the PKR-eIF2α Axis in Multiple Species.Vaccines · 2025Article
- The helicase domain of human Dicer prevents RNAi-independent activation of antiviral and inflammatory pathways.The EMBO journal · 2024Article
- Chemotherapy-Induced Senescence Reprogramming Promotes Nasopharyngeal Carcinoma Metastasis by circRNA-Mediated PKR Activation.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023Article
- Maladaptation after a virus host switch leads to increased activation of the pro-inflammatory NF-κB pathway.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Battle Royale: Innate Recognition of Poxviruses and Viral Immune Evasion.Biomedicines · 2021Review
- Review
- Glycogen synthase kinase (GSK)-3 and the double-strand RNA-dependent kinase, PKR: When two kinases for the common good turn bad.Biochimica et biophysica acta. Molecular cell research · 2020Review
- Review
- NF-κB Activation Promotes Alphavirus Replication in Mature Neurons.Journal of virology · 2019Article
- Binding of eEF1A2 to the RNA-dependent protein kinase PKR modulates its activity and promotes tumour cell survival.British journal of cancer · 2018Article
- Cytoplasmic RNA Granules and Viral Infection.Annual review of virology · 2014Article
- Dual activators of protein kinase R (PKR) and protein kinase R-like kinase PERK identify common and divergent catalytic targets.Chembiochem : a European journal of chemical biology · 2013Article
- The virion host shutoff RNase plays a key role in blocking the activation of protein kinase R in cells infected with herpes simplex virus 1.Journal of virology · 2013Article
- Review
- Large G3BP-induced granules trigger eIF2α phosphorylation.Molecular biology of the cell · 2012Article
- Increased expression of the dsRNA-activated protein kinase PKR in breast cancer promotes sensitivity to doxorubicin.PloS one · 2012Article
- Virus infection rapidly activates the P58(IPK) pathway, delaying peak kinase activation to enhance viral replication.Virology · 2011Article
- Double-stranded RNA-activated protein kinase regulates early innate immune responses during respiratory syncytial virus infection.Journal of interferon & cytokine research : the official journal of the International Society for Interferon and Cytokine Research · 2010Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The double stranded RNA-dependent protein kinase (PKR), in addition to its role as a translational controlling factor, is a key transcriptional regulator exerting antiviral and antitumoral activities. We have previously shown that induction of NF-kappaB by PKR is involved in apoptosis commitment and this process is mediated through activation of the IKK complex. To gain insights into the mechanism of activation of NF-kappaB by PKR, we have analysed the domains of PKR involved in IKK activation and subsequent NF-kappaB induction. In PKR(0/0) cells infected with a collection of vaccinia virus (VV) recombinants expressing different mutant forms of PKR, we found that only PKR forms conserving the catalytic activity are able to activate NF-kappaB. An inactive PKR mutant (K296R), was unable to induce NF-kappaB activation despite full expression of the protein in a wide range of concentrations, as defined by Western blot, EMSA, IKK kinase activity and NF-kappaB transactivation assays. Moreover, the mutant PKR (K296R) acts as a dominant negative of PKR-induced eIF-2alpha phosphorylation and NF-kappaB activation. However, PKR mutants unable to activate NF-kappaB still retain their ability to associate with the IKK complex, as confirmed by immunoprecipitation analysis. We conclude that the catalytic activity of PKR and not only a protein-protein interaction with the IKK complex, is needed for activation of the transcription factor NF-kappaB.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.