ArticleNucleic acids research2015
The eIF3 complex of Leishmania-subunit composition and mode of recruitment to different cap-binding complexes.
Article in Nucleic acids research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed.
- eIF3 musketeers: loyal in health, rogue in disease, and redeemed by therapeutic targeting.The EMBO journal · 2026Review
- The related EIF4G3 and EIF4G4 initiation factors from Leishmania: dissimilar modes of action during translation revealed by a comparative proteomic approach.Parasites & vectors · 2026Article
- AC005034.3/hsa-miR-126-5p/EIF3H axis: bioinformatics analysis, expression validation, and association with prognosis and immunosuppressive microenvironment in pancreatic adenocarcinoma.Frontiers in cell and developmental biology · 2026Article
- Article
- LeishIF3d is a non-canonical cap-binding protein inFrontiers in molecular biosciences · 2023Article
- Analysis of domain organization and functional signatures of trypanosomatid keIF4Gs.Molecular and cellular biochemistry · 2022Article
- Experimental evolution links post-transcriptional regulation to Leishmania fitness gain.PLoS pathogens · 2022Article
- Profilin is involved in G1 to S phase progression and mitotic spindle orientation during Leishmania donovani cell division cycle.PloS one · 2022Article
- Distinct mRNA and protein interactomes highlight functional differentiation of major eIF4F-like complexes fromFrontiers in molecular biosciences · 2022Article
- The EIF4E1-4EIP cap-binding complex of Trypanosoma brucei interacts with the terminal uridylyl transferase TUT3.PloS one · 2021Article
- Structural Differences in Translation Initiation between Pathogenic Trypanosomatids and Their Mammalian Hosts.Cell reports · 2020Article
- eIF4E and Interactors from Unicellular Eukaryotes.International journal of molecular sciences · 2020Review
- The suppressive cap-binding complex factor 4EIP is required for normal differentiation.Nucleic acids research · 2018Article
- The Jigsaw Puzzle of mRNA Translation Initiation in Eukaryotes: A Decade of Structures Unraveling the Mechanics of the Process.Annual review of biophysics · 2018Article
- Article
- The Role of Cytoplasmic mRNA Cap-Binding Protein Complexes in Trypanosoma brucei and Other Trypanosomatids.Pathogens (Basel, Switzerland) · 2017Review
- Molecular Landscape of the Ribosome Pre-initiation Complex during mRNA Scanning: Structural Role for eIF3c and Its Control by eIF5.Cell reports · 2017Article
- Untranslated regions of mRNA and their role in regulation of gene expression in protozoan parasites.Journal of biosciences · 2017Review
- The eIF3 complex ofRNA (New York, N.Y.) · 2017Article
- Article
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6 authors.
Funding
Abstract
Eukaryotic initiation factor 3 (eIF3) is a multi-protein complex and a key participant in the assembly of the translation initiation machinery. In mammals, eIF3 comprises 13 subunits, most of which are characterized by conserved structural domains. The trypanosomatid eIF3 subunits are poorly conserved. Here, we identify 12 subunits that comprise the Leishmania eIF3 complex (LeishIF3a-l) by combining bioinformatics with affinity purification and mass spectrometry analyses. These results highlight the strong association of LeishIF3 with LeishIF1, LeishIF2 and LeishIF5, suggesting the existence of a multi-factor complex. In trypanosomatids, the translation machinery is tightly regulated in the different life stages of these organisms as part of their adaptation and survival in changing environments. We, therefore, addressed the mechanism by which LeishIF3 is recruited to different mRNA cap-binding complexes. A direct interaction was observed in vitro between the fully assembled LeishIF3 complex and recombinant LeishIF4G3, the canonical scaffolding protein of the cap-binding complex in Leishmania promastigotes. We further highlight a novel interaction between the C-terminus of LeishIF3a and LeishIF4E1, the only cap-binding protein that efficiently binds the cap structure under heat shock conditions, anchoring a complex that is deficient of any MIF4G-based scaffolding subunit.
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