ArticleStructure (London, England : 1993)2013
Structural analysis of the DAP5 MIF4G domain and its interaction with eIF4A.
Article in Structure (London, England : 1993), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
What it found
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Who cites it
24 citing papers in PubMed, 42 citations in OpenAlex.
- Eukaryotic translation initiation factor 4F: functional properties and physiological role.Nucleic acids research · 2025Review
- Eukaryotic initiation factors eIF4F and eIF4B promote translation termination upon closed-loop formation.Nucleic acids research · 2025Article
- Modeling the structure and DAP5-binding site of the FGF-9 5'-UTR RNA utilized in cap-independent translation.RNA (New York, N.Y.) · 2024Article
- Non-canonical mRNA translation initiation in cell stress and cancer.NAR cancer · 2024Review
- Loss-of-function cancer-linked mutations in the EIF4G2 non-canonical translation initiation factor.Life science alliance · 2024Article
- Regulation and mechanisms of action of RNA helicases.RNA biology · 2024Review
- Specific mechanisms of translation initiation in higher eukaryotes: the eIF4G2 story.RNA (New York, N.Y.) · 2023Review
- Eukaryotic translation initiation factor eIF4G2 opens novel paths for protein synthesis in development, apoptosis and cell differentiation.Cell proliferation · 2023Review
- The metaphorical swiss army knife: The multitude and diverse roles of HEAT domains in eukaryotic translation initiation.Nucleic acids research · 2022Review
- Phosphorylation of Eukaryotic Initiation Factor 4G1 (eIF4G1) at Ser1147 Is Specific for eIF4G1 Bound to eIF4E in Delayed Neuronal Death after Ischemia.International journal of molecular sciences · 2022Article
- 5'-UTR recruitment of the translation initiation factor eIF4GI or DAP5 drives cap-independent translation of a subset of human mRNAs.The Journal of biological chemistry · 2020Article
- Translation Regulation by eIF2α Phosphorylation and mTORC1 Signaling Pathways in Non-Communicable Diseases (NCDs).International journal of molecular sciences · 2020Review
- Crystal structure of the MIF4G domain of the Trypanosoma cruzi translation initiation factor EIF4G5.Acta crystallographica. Section F, Structural biology communications · 2019Article
- The mammalian host protein DAP5 facilitates the initial round of translation of Coxsackievirus B3 RNA.The Journal of biological chemistry · 2019Article
- Identification and Analysis of OVATE Family Members from Genome of the Early Land Plants Provide Insights into Evolutionary History of OFP Family and Function.Journal of molecular evolution · 2018Article
- Ribosomal RACK1:Protein Kinase C βII Phosphorylates Eukaryotic Initiation Factor 4G1 at S1093 To Modulate Cap-Dependent and -Independent Translation Initiation.Molecular and cellular biology · 2018Article
- A widespread alternate form of cap-dependent mRNA translation initiation.Nature communications · 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
- Cleavage of DAP5 by coxsackievirus B3 2A protease facilitates viral replication and enhances apoptosis by altering translation of IRES-containing genes.Cell death and differentiation · 2016Article
- Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
Abstract
Death-associated protein 5 (DAP5/p97) is a homolog of the eukaryotic initiation factor 4G (eIF4G) that promotes the IRES-driven translation of multiple cellular mRNAs. Central to its function is the middle domain (MIF4G), which recruits the RNA helicase eIF4A. The middle domain of eIF4G consists of tandem HEAT repeats that coalesce to form a solenoid-type structure. Here, we report the crystal structure of the DAP5 MIF4G domain. Its overall fold is very similar to that of eIF4G; however, significant conformational variations impart distinct surface properties that could explain the observed differences in IRES binding between the two proteins. Interestingly, quantitative analysis of the DAP5-eIF4A interaction using isothermal titration calorimetry reveals a 10-fold lower affinity than with the eIF4G-eIF4A interaction that appears to affect their ability to stimulate eIF4A RNA unwinding activity in vitro. This difference in stability of the complex may have functional implications in selecting the mode of translation initiation.
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Registered trials
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.