ArticleThe Journal of biological chemistry2013
Spectrin domain of eukaryotic initiation factor 3a is the docking site for formation of the a:b:i:g subcomplex.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 33 citations in OpenAlex.
- Domain architecture of plant eukaryotic translation initiation factor 3 subunit E governs interaction with translational cis-elements to regulatepollen tube growth.The Plant cell · 2026Article
- eIF3: a critical player in mRNA recruitment to the ribosome with emerging roles across translation.Biochemical Society transactions · 2025Review
- mActa pharmaceutica Sinica. B · 2025Review
- The eIF3a translational control axis in the Wnt/β-catenin signaling pathway and colon tumorigenesis.Cancer letters · 2024Article
- Proteomic profiling of eIF3a conditional knockout mice.Frontiers in molecular biosciences · 2023Article
- Eukaryotic initiation factor 4F promotes a reorientation of eukaryotic initiation factor 3 binding on the 5' and the 3' UTRs of barley yellow dwarf virus mRNA.Nucleic acids research · 2022Article
- eIF3a regulation of mTOR signaling and translational control via HuR in cellular response to DNA damage.Oncogene · 2022Article
- A structural inventory of native ribosomal ABCE1-43S pre-initiation complexes.The EMBO journal · 2021Article
- Translational regulation of Chk1 expression by eIF3a via interaction with the RNA-binding protein HuR.The Biochemical journal · 2020Article
- Engineered transient and stable overexpression of translation factors eIF3i and eIF3c in CHOK1 and HEK293 cells gives enhanced cell growth associated with increased c-Myc expression and increased recombinant protein synthesis.Metabolic engineering · 2020Article
- Adapted formaldehyde gradient cross-linking protocol implicates human eIF3d and eIF3c, k and l subunits in the 43S and 48S pre-initiation complex assembly, respectively.Nucleic acids research · 2020Article
- eIF3a Regulation of NHEJ Repair Protein Synthesis and Cellular Response to Ionizing Radiation.Frontiers in cell and developmental biology · 2020Article
- Single-nucleotide polymorphisms in a short basic motif in the ABC transporter ABCG2 disable its trafficking out of endoplasmic reticulum and reduce cell resistance to anticancer drugs.The Journal of biological chemistry · 2019Article
- eIF3: a factor for human health and disease.RNA biology · 2018Review
- Embraced by eIF3: structural and functional insights into the roles of eIF3 across the translation cycle.Nucleic acids research · 2017Article
- The eIF3 complex ofRNA (New York, N.Y.) · 2017Article
- Human eIF3b and eIF3a serve as the nucleation core for the assembly of eIF3 into two interconnected modules: the yeast-like core and the octamer.Nucleic acids research · 2016Article
- Assembly of eIF3 Mediated by Mutually Dependent Subunit Insertion.Structure (London, England : 1993) · 2016Article
- ABCE1 is essential for S phase progression in human cells.Cell cycle (Georgetown, Tex.) · 2016Article
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5 authors at 3 institutions in 1 country.
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Abstract
eIF3a (eukaryotic translation initiation factor 3a), one of the core subunits of the eIF3 complex, has been implicated in regulating translation of different mRNAs and in tumorigenesis. A subcomplex consisting of eIF3a, eIF3b, eIF3g, and eIF3i (eIF3(a:b:i:g)) has also been identified. However, how eIF3a participates in translational regulation and in formation of the eIF3(a:b:i:g) subcomplex remain to be solved. In this study, we used the tandem affinity purification approach in combination with tandem MS/MS and identified the spectrin domain of eIF3a as the docking site for the formation of eIF3(a:b:i:g) subcomplex. Although eIF3b and eIF3i bind concurrently to the spectrin domain of eIF3a within ∼10-15 amino acids apart, eIF3g binds to eIF3a indirectly via binding to the carboxyl-terminal domain of eIF3b. The binding of eIF3b to the spectrin domain of eIF3a occurs in its RNA recognition motif domain where eIF3j also binds in a mutually exclusive manner. Together, we conclude that the spectrin domain of eIF3a is responsible for the formation of eIF3(a:b:i:g) subcomplex and, because of mutually exclusive nature of bindings of eIF3a and eIF3j to eIF3b, different subcomplexes of eIF3 likely exist and may perform noncanonical functions in translational regulation.
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