ArticleNucleic acids research2022
Quaternary organization of the human eEF1B complex reveals unique multi-GEF domain assembly.
Article in Nucleic acids research, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- The ER anchoring and abundance of the EEF1B complex is affected by tissue-specific alternative EEF1D splicing.Life science alliance · 2026Article
- HaDeX2: multi-dimensional analysis of hydrogen-deuterium exchange mass spectrometry data.Bioinformatics (Oxford, England) · 2026Article
- Cysteine-enabled cleavability to advance cross-linking mass spectrometry for global analysis of endogenous protein-protein interactions.Nature communications · 2025Article
- CDR2 is a dynein adaptor recruited by kinectin to regulate ER sheet organization.The Journal of cell biology · 2025Article
- Multidimensional Regulatory Mechanisms and Targeting Strategies of the eEF1 Family in RNA Virus Infection.Viruses · 2025Review
- HRaDeX: R Package and Web Server for Computing High-Resolution Deuterium Uptake Rates for HDX-MS Data.Journal of proteome research · 2025Article
- EEF1B2 regulates bone marrow-derived mesenchymal stem cells bone-fat balance via Wnt/β-catenin signaling.Cellular and molecular life sciences : CMLS · 2024Article
- Hidden Glutathione Transferases in the Human Genome.Biomolecules · 2023Article
- Reconstitution of Multi-Protein Complexes through Ribozyme-Assisted Polycistronic Co-Expression.ACS synthetic biology · 2023Article
- The eEF1 family of mammalian translation elongation factors.BBA advances · 2023Article
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10 authors.
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Abstract
Protein synthesis in eukaryotic cell is spatially and structurally compartmentalized that ensures high efficiency of this process. One of the distinctive features of higher eukaryotes is the existence of stable multi-protein complexes of aminoacyl-tRNA synthetases and translation elongation factors. Here, we report a quaternary organization of the human guanine-nucleotide exchange factor (GEF) complex, eEF1B, comprising α, β and γ subunits that specifically associate into a heterotrimeric form eEF1B(αβγ)3. As both the eEF1Bα and eEF1Bβ proteins have structurally conserved GEF domains, their total number within the complex is equal to six. Such, so far, unique structural assembly of the guanine-nucleotide exchange factors within a stable complex may be considered as a 'GEF hub' that ensures efficient maintenance of the translationally active GTP-bound conformation of eEF1A in higher eukaryotes.
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