ArticleScientific reports2018
Differential effects of SUMO1 and SUMO3 on PKR activation and stability.
Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 17 citations in OpenAlex.
- Ubiquitin and ubiquitin-like modifications in the endoplasmic reticulum stress response.The FEBS journal · 2026Review
- SUMOylated Golgin45 associates with PML-NB to transcriptionally regulate lipid metabolism genes during heat shock stress.Communications biology · 2024Article
- Paradoxes of Cellular SUMOylation Regulation: A Role of Biomolecular Condensates?Pharmacological reviews · 2023Review
- Review
- PKR activity modulation by phosphomimetic mutations of serine residues located three aminoacids upstream of double-stranded RNA binding motifs.Scientific reports · 2021Article
- Inhibition of PKR by Viruses.Frontiers in microbiology · 2021Review
- Crosstalk Between SUMO and Ubiquitin-Like Proteins: Implication for Antiviral Defense.Frontiers in cell and developmental biology · 2021Review
- 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
- SUMO and Cytoplasmic RNA Viruses: From Enemies to Best Friends.Advances in experimental medicine and biology · 2020Review
- The Leader Protein of Theiler's Virus Prevents the Activation of PKR.Journal of virology · 2019Article
- Optimization of Extraction Technology of Majun Mupakhi Ela and its Effect on Hydrocortisone-induced Kidney Yang Deficiency in Mice.Scientific reports · 2019Article
- Rhabdoviruses, Antiviral Defense, and SUMO Pathway.Viruses · 2018Review
- Innate Immune Detection of Cardioviruses and Viral Disruption of Interferon Signaling.Frontiers in microbiology · 2018Review
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
Double-stranded RNA (dsRNA)-dependent protein kinase (PKR) is a serine/threonine kinase that exerts its own phosphorylation and the phosphorylation of the α subunit of the protein synthesis initiation factor eIF-2α. PKR was identified as a target of SUMOylation and the triple PKR-SUMO deficient mutant on Lysine residues K60-K150-K440 has reduced PKR activity. We report that SUMO1 and SUMO3 expression exert differential effects on PKR localization, activation and stability. SUMO1 or SUMO3 did not alter the repartition of PKR in the cytoplasm and the nucleus. However, in SUMO3-expressing cells PKR was found more concentrated around the perinuclear membrane and was recruited from small speckles to nuclear dots. Interestingly, SUMO1 expression alone resulted in PKR and eIF-2α activation, whereas SUMO3 reduced PKR and eIF-2α activation upon viral infection or dsRNA transfection. In addition, encephalomyocarditis virus (EMCV) enhanced PKR conjugation to SUMO1 and SUMO3 but only SUMO3 expression promoted caspase-dependent EMCV-induced PKR degradation. Furthermore, the higher EMCV-induced PKR activation by SUMO1 was correlated with an inhibition of EMCV. Importantly SUMO1, by inducing PKR activation in the absence of viral infection, and SUMO3, by counteracting both PKR activation and stability upon viral infection, shed a new light on the differential effects of SUMO-modified 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.