ArticlePloS one2009
A variant mimicking hyperphosphorylated 4E-BP inhibits protein synthesis in a sea urchin cell-free, cap-dependent translation system.
Article in PloS one, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 34 citations in OpenAlex.
- Protein translation paradox: Implications in translational regulation of aging.Frontiers in cell and developmental biology · 2023Review
- A predictive coarse-grained model for position-specific effects of post-translational modifications.Biophysical journal · 2021Article
- Translational Control of Canonical and Non-Canonical Translation Initiation Factors at the Sea Urchin Egg to Embryo Transition.International journal of molecular sciences · 2019Article
- Site-specific phosphorylation regulates the structure and function of an intrinsically disordered domain of the glucocorticoid receptor.Scientific reports · 2017Article
- Modulation of Intrinsically Disordered Protein Function by Post-translational Modifications.The Journal of biological chemistry · 2016Review
- Cyclin B Translation Depends on mTOR Activity after Fertilization in Sea Urchin Embryos.PloS one · 2016Article
- Folding of an intrinsically disordered protein by phosphorylation as a regulatory switch.Nature · 2015Article
- An eIF4E-interacting peptide induces cell death in cancer cell lines.Cell death & disease · 2014Article
- Modelization of the regulation of protein synthesis following fertilization in sea urchin shows requirement of two processes: a destabilization of eIF4E:4E-BP complex and a great stimulation of the 4E-BP-degradation mechanism, both rapamycin-sensitive.Frontiers in genetics · 2014Article
- mTOR Signaling in Protein Translation Regulation: Implications in Cancer Genesis and Therapeutic Interventions.Molecular biology international · 2014Review
- Tracking a refined eIF4E-binding motif reveals Angel1 as a new partner of eIF4E.Nucleic acids research · 2013Article
- Anti-oncogenic potential of the eIF4E-binding proteins.Oncogene · 2013Review
- Hydrogen peroxide induces stress granule formation independent of eIF2α phosphorylation.Biochemical and biophysical research communications · 2012Article
- mRNA-selective translation induced by FSH in primary Sertoli cells.Molecular endocrinology (Baltimore, Md.) · 2012Article
- The translational repressor 4E-BP called to order by eIF4E: new structural insights by SAXS.Nucleic acids research · 2011Article
- Vasa genes: emerging roles in the germ line and in multipotent cells.BioEssays : news and reviews in molecular, cellular and developmental biology · 2010Article
- Fibroblast growth factor 1 induced during myogenesis by a transcription-translation coupling mechanism.Nucleic acids research · 2009Article
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
background4E-BP is a translational inhibitor that binds to eIF4E to repress cap-dependent translation initiation. This critical protein:protein interaction is regulated by the phosphorylation of 4E-BP. Hypophosphorylated 4E-BP binds to eIF4E and inhibits cap-dependent translation, whereas hyperphosphorylated forms do not. While three 4E-BP proteins exist in mammals, only one gene encoding for 4E-BP is present in the sea urchin genome. The protein product has a highly conserved core domain containing the eIF4E-binding domain motif (YxxxxLPhi) and four of the regulatory phosphorylation sites. METHODOLOGY/PRINCIPAL
findingsUsing a sea urchin cell-free cap-dependent translation system prepared from fertilized eggs, we provide the first direct evidence that the sea urchin 4E-BP inhibits cap-dependent translation. We show here that a sea urchin 4E-BP variant, mimicking phosphorylation on four core residues required to abrogate binding to eIF4E, surprisingly maintains physical association to eIF4E and inhibits protein synthesis. CONCLUSIONS/SIGNIFICANCE: Here, we examine the involvement of the evolutionarily conserved core domain and phosphorylation sites of sea urchin 4E-BP in the regulation of eIF4E-binding. These studies primarily demonstrate the conserved activity of the 4E-BP translational repressor and the importance of the eIF4E-binding domain in sea urchin. We also show that a variant mimicking hyperphosphorylation of the four regulatory phosphorylation sites common to sea urchin and human 4E-BP is not sufficient for release from eIF4E and translation promotion. Therefore, our results suggest that there are additional mechanisms to that of phosphorylation at the four critical sites of 4E-BP that are required to disrupt binding to eIF4E.
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