ReviewEuropean journal of biochemistry2002
Does phosphorylation of the cap-binding protein eIF4E play a role in translation initiation?
Review in European journal of biochemistry, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 126 papers.
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Who cites it
126 citing papers in PubMed, 306 citations in OpenAlex.
- ASFV MGF110-7L Inhibits eIF4G1 Expression via Endoplasmic Reticulum Stress to Block Host Translation.Viruses · 2026Article
- Arsenic Trioxide and the MNK1 Inhibitor AUM001 Exert Synergistic Anti-Glioblastoma Effects by Modulating Key Translational, Cell Cycle, and Transmembrane Transport Pathways.Brain sciences · 2026Article
- The many ways to inhibit translation by Sorafenib in liver cancer cells.Molecular and cellular biochemistry · 2026Article
- Article
- Design, synthesis and biological evaluation of MNK-PROTACs.Molecular diversity · 2024Article
- Trinucleotide cap analogs with triphosphate chain modifications: synthesis, properties, and evaluation as mRNA capping reagents.Nucleic acids research · 2024Article
- Article
- Molecular signatures of diapause in the Asian longhorned beetle: Gene expression.Current research in insect science · 2023Article
- High-throughput translational profiling with riboPLATE-seq.Scientific reports · 2022Article
- Spatiotemporally resolved protein synthesis as a molecular framework for memory consolidation.Trends in neurosciences · 2022Review
- Control of the eIF4E activity: structural insights and pharmacological implications.Cellular and molecular life sciences : CMLS · 2021Review
- Immunization and Drug Metabolizing Enzymes: Focus on Hepatic Cytochrome P450 3A.Expert review of vaccines · 2021Article
- Pharmacological Manipulation of Translation as a Therapeutic Target for Chronic Pain.Pharmacological reviews · 2021Review
- Newcastle Disease virus infection activates PI3K/Akt/mTOR and p38 MAPK/Mnk1 pathways to benefit viral mRNA translation via interaction of the viral NP protein and host eIF4E.PLoS pathogens · 2020Article
- Deciphering the mechanistic effects of eIF4E phosphorylation on mRNA-cap recognition.Protein science : a publication of the Protein Society · 2020Article
- Infection by the Protozoan ParasiteFrontiers in cellular and infection microbiology · 2020Article
- Cell Fate Control by Translation: mRNA Translation Initiation as a Therapeutic Target for Cancer Development and Stem Cell Fate Control.Biomolecules · 2019Review
- Translating from cancer to the brain: regulation of protein synthesis by eIF4F.Learning & memory (Cold Spring Harbor, N.Y.) · 2019Review
- Translational Control in Cancer.Cold Spring Harbor perspectives in biology · 2019Review
- Monitoring flux in signalling pathways through measurements of 4EBP1-mediated eIF4F complex assembly.BMC biology · 2019Article
66 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Eukaryotic initiation factor 4E (eIF4E) plays an important role in mRNA translation by binding the 5'-cap structure of the mRNA and facilitating the recruitment to the mRNA of other translation factors and the 40S ribosomal subunit. eIF4E can interact either with the scaffold protein eIF4G or with repressor proteins termed eIF4E-binding proteins (4E-BPs). High levels of expression can disrupt cellular growth control and are associated with human cancers. A fraction of the cellular eIF4E is found in the nucleus where it may play a role in the transport of certain mRNAs to the cytoplasm. eIF4E undergoes regulated phosphorylation (at Ser209) by members of the Mnk group of kinases, which are activated by multiple MAP kinases (hence Mnk = MAP-kinase signal integrating kinase). The functional significance of its phosphorylation has been the subject of considerable interest. Recent genetic studies in Drosophila point to a key role for phosphorylation of eIF4E in growth and viability. Initial structural data suggested that phosphorylation of Ser209 might allow formation of a salt bridge with a basic residue (Lys159) that would clamp eIF4E onto the mRNA and increase its affinity for ligand. However, more recent structural data place Ser209 too far away from Lys159 to form such an interaction, and biophysical studies indicate that phosphorylation actually decreases the affinity of eIF4E for cap or capped RNA. The implications of these studies are discussed in the light of other, in vitro and in vivo, investigations designed to address the role of eIF4E phosphorylation in mRNA translation or its control.
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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.