ArticleProtein science : a publication of the Protein Society2020
Deciphering the mechanistic effects of eIF4E phosphorylation on mRNA-cap recognition.
Article in Protein science : a publication of the Protein Society, 2020. 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.
- Article
- Beyond the Sequence: Chemical and Topological Design and Innovations in mRNA Therapeutics.Chemical reviews · 2026Review
- Sortase-Mediated Fluorescent Labeling of eIF4E for Investigating Translation Initiation Mechanisms.Biochemistry · 2025Article
- An evolutionarily conserved phosphoserine-arginine salt bridge in the interface between ribosomal proteins uS4 and uS5 regulates translational accuracy in Saccharomyces cerevisiae.Nucleic acids research · 2024Article
- The role of eIF4F-driven mRNA translation in regulating the tumour microenvironment.Nature reviews. Cancer · 2023Review
- Pathophysiology of obesity and its associated diseases.Acta pharmaceutica Sinica. B · 2023Review
- Proteomic screening identifies RPLp2 as a specific regulator for the translation of coronavirus.International journal of biological macromolecules · 2023Article
- Substrate-Based Design of Cytosolic Nucleotidase IIIB Inhibitors and Structural Insights into Inhibition Mechanism.Pharmaceuticals (Basel, Switzerland) · 2022Article
- Control of the eIF4E activity: structural insights and pharmacological implications.Cellular and molecular life sciences : CMLS · 2021Review
- Translational control in neurovascular brain development.Royal Society open science · 2021Review
- The Use of Peptides in the Treatment of Fragile X Syndrome: Challenges and Opportunities.Frontiers in psychiatry · 2021Article
- The MNK1/2-eIF4E Axis as a Potential Therapeutic Target in Melanoma.International journal of molecular sciences · 2020Review
- Deciphering the mechanistic effects of eIF4E phosphorylation on mRNA-cap recognition.Protein science : a publication of the Protein Society · 2020Article
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2 authors.
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Abstract
The mRNA cap-binding oncoprotein "eIF4E" is phosphorylated at residue S209 by Mnk kinases, and is closely associated with tumor development and progression. Despite being well-established, mechanistic details at the molecular level of mRNA recognition by eIF4E due to phosphorylation have not been clearly elucidated. We investigated this through molecular modeling and simulations of the S209 phosphorylated derivative of eIF4E and explored the associated implication on the binding of the different variants of mRNA-cap analogs. A key feature that emerges as a result of eIF4E phosphorylation is a salt-bridge network between the phosphorylated S209 (pS209) and a specific pair of lysine residues (K159 and K162) within the cap-binding interface on eIF4E. This interaction linkage stabilizes the otherwise dynamic C-terminal region of the protein, resulting in the attenuation of the overall plasticity and accessibility of the binding pocket. The pS209-K159 salt-bridge also results in an energetically less favorable environment for the bound mRNA-cap primarily due to electrostatic repulsion between the negative potentials from the phosphates in the cap and those appearing as a result of phosphorylation of S209. These observations collectively imply that the binding of the mRNA-cap will be adversely affected in the phosphorylated derivative of eIF4E. We propose a mechanistic model highlighting the role of eIF4E phosphorylation as a regulatory tool in modulating eIF4E: mRNA-cap recognition and its potential impact on translation initiation.
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