ArticleProceedings of the National Academy of Sciences of the United States of America2006
Tyrosine phosphorylation acts as a molecular switch to full-scale activation of the eIF2alpha RNA-dependent protein kinase.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
43 citing papers in PubMed, 77 citations in OpenAlex.
- PKR condensation at viral replication complexes initiates its activation.Cell reports · 2026Article
- Roles and Applications of Circular RNA in Virus Infection.International journal of molecular sciences · 2025Review
- Respiratory syncytial virus (RSV) enhances translation of virus-resembling AU-rich host transcripts.Virology journal · 2025Article
- Activation of PKR by a short-hairpin RNA.Scientific reports · 2024Article
- Activation of PKR by a short-hairpin RNA.bioRxiv : the preprint server for biology · 2024Article
- Interaction between Sars-CoV-2 structural proteins and host cellular receptors: From basic mechanisms to clinical perspectives.Advances in protein chemistry and structural biology · 2022Review
- Mechanism of herpesvirus protein kinase UL13 in immune escape and viral replication.Frontiers in immunology · 2022Review
- Induction and Evasion of Type-I Interferon Responses during Influenza A Virus Infection.Cold Spring Harbor perspectives in medicine · 2021Review
- Activation of dsRNA-Dependent Protein Kinase R by miR-378 Sustains Metabolic Inflammation in Hepatic Insulin Resistance.Diabetes · 2021Article
- 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
- An integrated stress response via PKR suppresses HER2+ cancers and improves trastuzumab therapy.Nature communications · 2019Article
- Mechanism mediated by a noncoding RNA, nc886, in the cytotoxicity of a DNA-reactive compound.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Adenovirus VA RNAI Blocks ASC Oligomerization and Inhibits NLRP3 Inflammasome Activation.Frontiers in immunology · 2019Article
- Phosphorylable tyrosine residue 162 in the double-stranded RNA-dependent kinase PKR modulates its interaction with SUMO.Scientific reports · 2017Article
- The protein activator of protein kinase R, PACT/RAX, negatively regulates protein kinase R during mouse anterior pituitary development.The FEBS journal · 2015Article
- Novel RNA Duplex Locks HIV-1 in a Latent State via Chromatin-mediated Transcriptional Silencing.Molecular therapy. Nucleic acids · 2015Article
- Activation of the double-stranded RNA-dependent protein kinase PKR by small ubiquitin-like modifier (SUMO).The Journal of biological chemistry · 2014Article
- Hepatic mitochondrial and ER stress induced by defective PPARα signaling in the pathogenesis of hepatic steatosis.American journal of physiology. Endocrinology and metabolism · 2014Article
- The eIF2α kinases: their structures and functions.Cellular and molecular life sciences : CMLS · 2013Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Phosphorylation of the alpha-subunit of translation eukaryotic initiation factor-2 (eIF2) leads to the inhibition of protein synthesis in response to diverse conditions of stress. Serine/threonine RNA-dependent protein kinase (PKR) is an eIF2alpha kinase family member induced by type I IFN and activated in response to dsRNA or virus infection. Herein, we demonstrate that human PKR is a dual specificity kinase phosphorylated at Y101, Y162 and Y293 in vitro and in vivo. Site-specific tyrosine phosphorylation is essential for efficient dsRNA-binding, dimerization, kinase activation and eIF2alpha phosphorylation of PKR. Biologically, tyrosine phosphorylation of PKR mediates the antiviral and antiproliferative properties of the kinase through its ability to control translation. Our data demonstrate an important role of tyrosine phosphorylation in biochemical and biological processes caused or mediated by the activation of the eIF2alpha kinase PKR.
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Registered trials
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.