ArticlePloS one2012
PKCα binds G3BP2 and regulates stress granule formation following cellular stress.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 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
32 citing papers in PubMed, 55 citations in OpenAlex.
- Research Progress on the Biological Function, Disease-Driving Mechanism and Clinical Targeting Strategies of G3BP2.Molecules (Basel, Switzerland) · 2026Review
- Kinase regulation by liquid-liquid phase separation.Trends in cell biology · 2023Review
- African swine fever virus pS273R antagonizes stress granule formation by cleaving the nucleating protein G3BP1 to facilitate viral replication.The Journal of biological chemistry · 2023Article
- Article
- A proteomics approach identifies novel resident zebrafish Balbiani body proteins Cirbpa and Cirbpb.Developmental biology · 2022Article
- Stress granules safeguard against MAPK signaling hyperactivation by sequestering PKC/Pck2: new findings and perspectives.Current genetics · 2021Review
- Resveratrol and related stilbene derivatives induce stress granules with distinct clearance kinetics.Molecular biology of the cell · 2021Article
- MG53 suppresses tumor progression and stress granule formation by modulating G3BP2 activity in non-small cell lung cancer.Molecular cancer · 2021Article
- Stress granules inhibit fatty acid oxidation by modulating mitochondrial permeability.Cell reports · 2021Article
- Characterization of the Gene Expression Patterns in the Murine Liver Following Intramuscular Administration of Baculovirus.Gene expression · 2021Article
- Single-cell transcriptome landscape of ovarian cells during primordial follicle assembly in mice.PLoS biology · 2020Article
- Targeting stress granules: A novel therapeutic strategy for human diseases.Pharmacological research · 2020Review
- Fasnall Induces Atypically Transient Stress Granules Independently of FASN Inhibition.iScience · 2020Article
- Review
- Small Molecule Screen Reveals Joint Regulation of Stress Granule Formation and Lipid Droplet Biogenesis.Frontiers in cell and developmental biology · 2020Article
- Understanding the roles of stress granule during chemotherapy for patients with malignant tumors.American journal of cancer research · 2020Review
- Rasputin a decade on and more promiscuous than ever? A review of G3BPs.Biochimica et biophysica acta. Molecular cell research · 2019Review
- RNA interference may suppress stress granule formation by preventing argonaute 2 recruitment.American journal of physiology. Cell physiology · 2019Article
- Identification of PP1-Gadd34 substrates involved in the unfolded protein response using K-BIPS, a method for phosphatase substrate identification.Molecular omics · 2018Article
- Histone arginine demethylase JMJD6 is linked to stress granule assembly through demethylation of the stress granule-nucleating protein G3BP1.The Journal of biological chemistry · 2017Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein kinase C (PKC) isoforms regulate a number of processes crucial for the fate of a cell. In this study we identify previously unrecognized interaction partners of PKCα and a novel role for PKCα in the regulation of stress granule formation during cellular stress. Three RNA-binding proteins, cytoplasmic poly(A)(+) binding protein (PABPC1), IGF-II mRNA binding protein 3 (IGF2BP3), and RasGAP binding protein 2 (G3BP2) all co-precipitate with PKCα. RNase treatment abolished the association with IGF2BP3 and PABPC1 whereas the PKCα-G3BP2 interaction was largely resistant to this. Furthermore, interactions between recombinant PKCα and G3BP2 indicated that the interaction is direct and PKCα can phosphorylate G3BP2 in vitro. The binding is mediated via the regulatory domain of PKCα and the C-terminal RNA-binding domain of G3BP2. Both proteins relocate to and co-localize in stress granules, but not to P-bodies, when cells are subjected to stress. Heat shock-induced stress granule assembly and phosphorylation of eIF2α are suppressed following downregulation of PKCα by siRNA. In conclusion this study identifies novel interaction partners of PKCα and a novel role for PKCα in regulation of stress granules.
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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.