ArticleThe EMBO journal2001
Heterologous dimerization domains functionally substitute for the double-stranded RNA binding domains of the kinase PKR.
Article in The EMBO journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.
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Who cites it
51 citing papers in PubMed, 101 citations in OpenAlex.
- From Cellular Stress to Systemic Adaptation: The Circadian Clock and Stress Response at Cellular and Systemic Levels.International journal of molecular sciences · 2026Review
- Review
- Nucleic acid-protein condensates in innate immune signaling.The EMBO journal · 2023Review
- dsRNA-induced condensation of antiviral proteins modulates PKR activity.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- PKR and TLR3 trigger distinct signals that coordinate the induction of antiviral apoptosis.Cell death & disease · 2022Article
- Efficient production of protein complexes in mammalian cells using a poxvirus vector.PloS one · 2022Article
- Nuclear PKR in retinal neurons in the early stage of diabetic retinopathy in streptozotocin‑induced diabetic rats.Molecular medicine reports · 2021Article
- SARS-CoV-2 nucleocapsid protein impairs stress granule formation to promote viral replication.Cell discovery · 2021Article
- Review
- MAVERICC: Marker-free Vaccinia Virus Engineering of Recombinants through in vitro CRISPR/Cas9 Cleavage.Journal of molecular biology · 2021Article
- Review
- The search for a PKR code-differential regulation of protein kinase R activity by diverse RNA and protein regulators.RNA (New York, N.Y.) · 2019Review
- The unfolded protein response controls endoplasmic reticulum stress-induced apoptosis of MCF-7 cells via a high dose of vitamin C treatment.Molecular biology reports · 2019Article
- ADAR1: "Editor-in-Chief" of Cytoplasmic Innate Immunity.Frontiers in immunology · 2019Review
- Mechanism of Protein Kinase R Inhibition by Human Cytomegalovirus pTRS1.Journal of virology · 2017Article
- dsRNA Binding Domain of PKR Is Proteolytically Released by Enterovirus A71 to Facilitate Viral Replication.Frontiers in cellular and infection microbiology · 2017Article
- PKR Transduces MDA5-Dependent Signals for Type I IFN Induction.PLoS pathogens · 2016Article
- The Regulatory and Kinase Domains but Not the Interdomain Linker Determine Human Double-stranded RNA-activated Kinase (PKR) Sensitivity to Inhibition by Viral Non-coding RNAs.The Journal of biological chemistry · 2015Article
- Baculovirus protein PK2 subverts eIF2α kinase function by mimicry of its kinase domain C-lobe.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Protein-Binding Function of RNA-Dependent Protein Kinase Promotes Proliferation through TRAF2/RIP1/NF-κB/c-Myc Pathway in Pancreatic β cells.Molecular medicine (Cambridge, Mass.) · 2015Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
The protein kinase PKR (dsRNA-dependent protein kinase) phosphorylates the eukaryotic translation initiation factor eIF2alpha to downregulate protein synthesis in virus-infected cells. Two double-stranded RNA binding domains (dsRBDs) in the N-terminal half of PKR are thought to bind the activator double-stranded RNA, mediate dimerization of the protein and target PKR to the ribosome. To investigate further the importance of dimerization for PKR activity, fusion proteins were generated linking the PKR kinase domain to heterologous dimerization domains. Whereas the isolated PKR kinase domain (KD) was non-functional in vivo, expression of a glutathione S-transferase-KD fusion, or co-expression of KD fusions containing the heterodimerization domains of the Xlim-1 and Ldb1 proteins, restored PKR activity in yeast cells. Finally, coumermycin-mediated dimerization of a GyrB-KD fusion protein increased eIF2alpha phosphorylation and inhibited reporter gene translation in mammalian cells. These results demonstrate the critical importance of dimerization for PKR activity in vivo, and suggest that a primary function of double-stranded RNA binding to the dsRBDs of native PKR is to promote dimerization and activation of the kinase domain.
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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.