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| eIF4A | |
|---|---|
| Name | eIF4A |
| Uniprot | P60842 |
| Organism | Homo sapiens |
eIF4A eIF4A is a highly conserved eukaryotic translation initiation factor that functions as an ATP-dependent RNA helicase. It is central to cap-dependent initiation and is studied across model organisms such as Saccharomyces cerevisiae, Caenorhabditis elegans, and Drosophila melanogaster, and in medical research at institutions like the National Institutes of Health and Max Planck Society. Research on eIF4A intersects with work by laboratories associated with the Howard Hughes Medical Institute, projects funded by the Wellcome Trust, and clinical studies at centers including Mayo Clinic.
eIF4A belongs to the DEAD-box family of helicases discovered in studies influenced by researchers from Cold Spring Harbor Laboratory, Harvard University, and University of Cambridge. Early characterization involved collaborations among groups at Massachusetts Institute of Technology, Stanford University, and the University of California, San Francisco, with biochemical techniques developed in the tradition of Kornberg Laboratory and Lasker Clinical Medical Research Award-associated research. eIF4A's role became prominent alongside discoveries related to the ribosome, the cap-dependent translation paradigm advanced in conferences at the Gordon Research Conferences and reviews in journals edited by figures connected to the Royal Society and American Association for the Advancement of Science.
The protein's core structure reflects motifs characterized in studies from Max Planck Institute of Biochemistry, showing canonical Walker A and Walker B motifs and conserved DEAD sequence identified in work influenced by John E. Walker. High-resolution structures obtained by groups at European Molecular Biology Laboratory and Institut Pasteur parallel techniques used in structural studies of the ATP synthase and RNA polymerase II. eIF4A hydrolyzes ATP during RNA duplex remodeling, a mechanism elucidated with X-ray crystallography and cryo-EM methods developed at Brookhaven National Laboratory and Lawrence Berkeley National Laboratory. Biochemical assays tracing ATP turnover reference approaches pioneered at Cold Spring Harbor Laboratory and analytical frameworks from International Union of Biochemistry and Molecular Biology meetings.
Eukaryotes encode multiple eIF4A isoforms such as EIF4A1, EIF4A2, and EIF4A3, with gene regulation studied in contexts linked to Human Genome Project efforts and annotations coordinated by National Center for Biotechnology Information and Ensembl. Genetic studies in Mus musculus and Zebrafish delineate isoform-specific expression patterns, using tools developed at Broad Institute and Wellcome Sanger Institute. Regulation of isoform expression engages transcription factors studied at Cold Spring Harbor Laboratory and chromatin regulators profiled by consortia like the ENCODE Project and epigenetics programs at European Bioinformatics Institute.
eIF4A participates in the eIF4F complex alongside eIF4E and eIF4G, a model refined in translational control studies at Cambridge University, Yale University, and University of Oxford. Its helicase activity unwinds 5' untranslated region secondary structures during scanning by the 43S pre-initiation complex, a process examined in comparative studies involving Escherichia coli ribosomal research and eukaryotic initiation analyses from EMBL-EBI collaborators. Functional assays connecting eIF4A to reinitiation and internal ribosome entry site studies draw on methodologies from European Molecular Biology Organization conferences and reviews by investigators associated with Cold Spring Harbor Laboratory.
eIF4A forms stable interactions with eIF4G and the regulatory protein eIF4B, with additional binding partners including PDCD4 and members of the exon junction complex studied in work at Johns Hopkins University and University College London. Proteomic surveys identifying eIF4A partners used mass spectrometry platforms from ProteomeXchange-affiliated centers and crosslinking approaches developed at Max Planck Institute for Biophysical Chemistry. Interactions with viral proteins from Human Immunodeficiency Virus and Hepatitis C virus have been mapped in collaborations involving Centers for Disease Control and Prevention and academic virology groups at Rockefeller University.
Post-translational modifications of eIF4A include phosphorylation and ubiquitination events characterized in signaling studies linked to the mTOR pathway, with mechanistic links explored by researchers at University of California, San Diego and Dana-Farber Cancer Institute. Kinases and ubiquitin ligases implicated in eIF4A regulation were identified using screens influenced by approaches from The Salk Institute and high-throughput platforms at European Molecular Biology Laboratory. Cellular stress responses modulating eIF4A activity have been analyzed in studies at National Institute of Allergy and Infectious Diseases and during investigations of stress granules associated with Alzheimer's disease and Parkinson's disease research groups.
Aberrant eIF4A function has been implicated in oncogenesis, with links to studies from Memorial Sloan Kettering Cancer Center, MD Anderson Cancer Center, and the National Cancer Institute. Natural products such as rocaglates (e.g., silvestrol) were characterized by collaborations involving University of Illinois and chemical biology groups at Scripps Research, leading to preclinical trials coordinated with pharmaceutical companies and translational centers like Fred Hutchinson Cancer Center. Antiviral strategies targeting eIF4A interactions are under investigation in consortiums including Bill & Melinda Gates Foundation-funded initiatives and public-private partnerships with manufacturers regulated by agencies such as the Food and Drug Administration.
Category:Translation factors