ArticleThe Journal of biological chemistry2020
Regulation of eukaryotic translation initiation factor 6 dynamics through multisite phosphorylation by GSK3.
Article in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 18 citations in OpenAlex.
- Five-layer systems analysis ofeLife · 2026Article
- Article
- Eukaryote initiation factor 6 modulates small-cell lung carcinoma plasticity via the integrin-FAK signaling axis.Nature communications · 2026Article
- High expression of eIF4A1 promotes angiogenesis through the NF‑κB/VEGFA pathway and predicts poor prognosis in gastric cancer.Oncology reports · 2025Article
- Data-Independent Acquisition (DIA)-Based Label-Free Redox Proteomics (DIALRP) Identifies Prominent Cysteine Oxidations in Translation Machinery in Prostate Cancer Cells Under Oxidative Stress.Journal of proteome research · 2025Article
- Sequestration of ribosomal subunits as inactive 80S by targeting eIF6 limits mitotic exit and cancer progression.Nucleic acids research · 2025Article
- p38α-eIF6-Nsun2 axis promotes ILC3's rapid response to protect host from intestinal inflammation.The Journal of experimental medicine · 2025Article
- The crosstalk between metabolism and translation.Cell metabolism · 2024Review
- Site-specific labeling of SBDS to monitor interactions with the 60S ribosomal subunit.Methods (San Diego, Calif.) · 2023Article
- Dynamic states of eIF6 and SDS variants modulate interactions with uL14 of the 60S ribosomal subunit.Nucleic acids research · 2023Article
- Relationship of micro-RNA, mRNA and eIF Expression in Tamoxifen-Adapted MCF-7 Breast Cancer Cells: Impact of miR-1972 on Gene Expression, Proliferation and Migration.Biomolecules · 2022Article
- Cytoplasmic eIF6 promotes OSCC malignant behavior through AKT pathway.Cell communication and signaling : CCS · 2021Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Eukaryotic translation initiation factor 6 (eIF6) is essential for the synthesis of 60S ribosomal subunits and for regulating the association of 60S and 40S subunits. A mechanistic understanding of how eIF6 modulates translation in response to stress, specifically starvation-induced stress, is lacking. We here show a novel mode of eIF6 regulation by glycogen synthase kinase 3 (GSK3) that is predominantly active in response to serum starvation. Both GSK3α and GSK3β phosphorylate human eIF6. Multiple residues in the C terminus of eIF6 are phosphorylated by GSK3 in a sequential manner. In response to serum starvation, eIF6 accumulates in the cytoplasm, and this altered localization depends on phosphorylation by GSK3. Disruption of eIF6 phosphorylation exacerbates the translation inhibitory response to serum starvation and stalls cell growth. These results suggest that eIF6 regulation by GSK3 contributes to the attenuation of global protein synthesis that is critical for adaptation to starvation-induced stress.
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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.