ArticleBiochemistry2019
Structural Basis of Protein Kinase R Autophosphorylation.
Article in Biochemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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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
21 citing papers in PubMed, 17 citations in OpenAlex.
- Regulatory mechanism of heme-regulated inhibitor through autophosphorylation-driven activation and heme-induced deactivation.Journal of biochemistry · 2026Article
- Phosphoproteomics Data-Driven Integrative Analysis of Autophosphorylation Sites in the Human Kinome.International journal of molecular sciences · 2026Article
- PKR condensation at viral replication complexes initiates its activation.Cell reports · 2026Article
- RNA triggers chronic stress during neuronal aging.bioRxiv : the preprint server for biology · 2025Article
- Cooperative role of PACT and ADAR1 in preventing aberrant PKR activation by self-derived double-stranded RNA.Nature communications · 2025Article
- Therapeutic application of circular RNA aptamers in a mouse model of psoriasis.Nature biotechnology · 2025Article
- Screening and experimental validation of modified Gandou Decoction-targeted inhibitors for alleviating AD components via network pharmacology, machine learning, and molecular dynamics simulation.Frontiers in pharmacology · 2025Article
- Dimerization Promotes PKR Activation by Modulating Energetics of αC Helix Conversion between Active and Inactive Conformations.The journal of physical chemistry. B · 2024Article
- The immune response to RNA suppresses nucleic acid synthesis by limiting ribose 5-phosphate.The EMBO journal · 2024Article
- RNA recognition by PKR during DNA virus infection.Journal of medical virology · 2024Review
- A critical evaluation of protein kinase regulation by activation loop autophosphorylation.eLife · 2023Article
- Nucleic acid-protein condensates in innate immune signaling.The EMBO journal · 2023Review
- Antagonism of Protein Kinase R by Large DNA Viruses.Pathogens (Basel, Switzerland) · 2022Review
- Signaling by the integrated stress response kinase PKR is fine-tuned by dynamic clustering.The Journal of cell biology · 2022Article
- Cellular origins of dsRNA, their recognition and consequences.Nature reviews. Molecular cell biology · 2022Review
- Temporal control of the integrated stress response by a stochastic molecular switch.Science advances · 2022Article
- Structural analysis of receptor-like kinase SOBIR1 reveals mechanisms that regulate its phosphorylation-dependent activation.Plant communications · 2022Article
- Genome-encoded cytoplasmic double-stranded RNAs, found inScience translational medicine · 2021Article
- Contribution of dsRBD2 to PKR Activation.ACS omega · 2021Article
- Inhibition of RNA-binding proteins with small molecules.Nature reviews. Chemistry · 2020Review
Corrections and comments
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Authors and funding
7 authors.
Funding
Abstract
The RNA-activated protein kinase, PKR, is a key mediator of the innate immunity response to viral infection. Viral double-stranded RNAs induce PKR dimerization and autophosphorylation. The PKR kinase domain forms a back-to-back dimer. However, intermolecular ( trans) autophosphorylation is not feasible in this arrangement. We have obtained PKR kinase structures that resolves this dilemma. The kinase protomers interact via the known back-to-back interface as well as a front-to-front interface that is formed by exchange of activation segments. Mutational analysis of the front-to-front interface support a functional role in PKR activation. Molecular dynamics simulations reveal that the activation segment is highly dynamic in the front-to-front dimer and can adopt conformations conducive to phosphoryl transfer. We propose a mechanism where back-to-back dimerization induces a conformational change that activates PKR to phosphorylate a "substrate" kinase docked in a front-to-front geometry. This mechanism may be relevant to related kinases that phosphorylate the eukaryotic initiation factor eIF2α.
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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.