ArticleMolecular and biochemical parasitology2011
The four trypanosomatid eIF4E homologues fall into two separate groups, with distinct features in primary sequence and biological properties.
Article in Molecular and biochemical parasitology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.
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53 citing papers in PubMed, 78 citations in OpenAlex.
- Med9 Is a Novel eIF4E-Interacting Protein inInternational journal of molecular sciences · 2026Article
- The related EIF4G3 and EIF4G4 initiation factors from Leishmania: dissimilar modes of action during translation revealed by a comparative proteomic approach.Parasites & vectors · 2026Article
- Trypanosoma cruzi eIF4E3- and eIF4E4-containing complexes bind different mRNAs and may sequester inactive mRNAs during nutritional stress.Nucleic acids research · 2025Article
- Trypanosomatid DRBD9s are likely to be eIF4B orthologues.Journal of biosciences · 2025Article
- Article
- Structural analysis of the Trypanosoma brucei EIF4E6/EIF4G5 complex reveals details of the interaction between unusual eIF4F subunits.Scientific reports · 2024Article
- Architecture, domain organization, and functional signatures of trypanosomatid keIF4A1s andJournal of biosciences · 2023Article
- Analysis of domain organization and functional signatures of trypanosomatid keIF4Gs.Molecular and cellular biochemistry · 2022Article
- Distinct mRNA and protein interactomes highlight functional differentiation of major eIF4F-like complexes fromFrontiers in molecular biosciences · 2022Article
- The translation initiation factor EIF4E5 from Leishmania: crystal structure and interacting partners.RNA biology · 2021Article
- Characterization of an Atypical eIF4E Ortholog inInternational journal of molecular sciences · 2021Article
- Distinct features of the Leishmania cap-binding protein LeishIF4E2 revealed by CRISPR-Cas9 mediated hemizygous deletion.PLoS neglected tropical diseases · 2021Article
- Taking a re-look at cap-binding signatures of the mRNA cap-binding protein eIF4E orthologues in trypanosomatids.Molecular and cellular biochemistry · 2021Review
- Computational study on the allosteric mechanism ofComputational and structural biotechnology journal · 2021Article
- The EIF4E1-4EIP cap-binding complex of Trypanosoma brucei interacts with the terminal uridylyl transferase TUT3.PloS one · 2021Article
- A newly identified Leishmania IF4E-interacting protein, Leish4E-IP2, modulates the activity of cap-binding protein paralogs.Nucleic acids research · 2020Article
- Organising the cell cycle in the absence of transcriptional control: Dynamic phosphorylation co-ordinates the Trypanosoma brucei cell cycle post-transcriptionally.PLoS pathogens · 2019Article
- Article
- Functional characterization of the translation initiation factor eIF4E of Echinococcus granulosus.Parasitology research · 2019Article
- Deletion of a Single LeishIF4E-3 Allele by the CRISPR-Cas9 System Alters Cell Morphology and Infectivity ofmSphere · 2019Article
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Authors and funding
11 authors at 2 institutions in 2 countries.
Funding
Abstract
Translation initiation in eukaryotes requires eIF4E, the cap binding protein, which mediates its function through an interaction with the scaffolding protein eIF4G, as part of the eIF4F complex. In trypanosomatids, four eIF4E homologues have been described but the specific function of each is not well characterized. Here, we report a study of these proteins in Trypanosoma brucei (TbEIF4E1 through 4). At the sequence level, they can be assigned to two groups: TbEIF4E1 and 2, similar in size to metazoan eIF4E1; and TbEIF4E3 and 4, with long N-terminal extensions. All are constitutively expressed, but whilst TbEIF4E1 and 2 localize to both the nucleus and cytoplasm, TbEIF4E3 and 4 are strictly cytoplasmic and are also more abundant. After knockdown through RNAi, TbEIF4E3 was the only homologue confirmed to be essential for viability of the insect procyclic form. In contrast, TbEIF4E1, 3 and 4 were all essential for the mammalian bloodstream form. Simultaneous RNAi knockdown of TbEIF4E1 and 2 caused cessation of growth and death in procyclics, but with a delayed impact on translation, whilst knockdown of TbEIF4E3 alone or a combined TbEIF4E1 and 4 knockdown led to substantial translation inhibition which preceded cellular death by several days, at least. Only TbEIF4E3 and 4 were found to interact with T. brucei eIF4G homologues; TbEIF4E3 bound both TbEIF4G3 and 4 whilst TbEIF4E4 bound only to TbEIF4G3. These results are consistent with TbEIF4E3 and 4 having distinct but relevant roles in initiation of protein synthesis.
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