ArticleJournal of molecular biology2012
AIMP3/p18 controls translational initiation by mediating the delivery of charged initiator tRNA to initiation complex.
Article in Journal of molecular biology, 2012. 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, 41 citations in OpenAlex.
- Variant-specific interaction of kinectin 1 with the multi-tRNA synthetase complex regulates ER sheet organization.iScience · 2026Article
- AIMP3 maintains cardiac homeostasis by regulating the editing activity of methionyl-tRNA synthetase.Nature cardiovascular research · 2025Article
- Lysyl-tRNA synthetase 1 promotes atherogenesis via autophagy-related secretion and inflammation.Scientific reports · 2025Article
- A methyltransferase-independent role for METTL1 in tRNA aminoacylation and oncogenic transformation.Molecular cell · 2025Article
- AIMP1: multifunctional regulator in physiology and pathology with therapeutic implications.PeerJ · 2025Review
- Article
- Solution X-ray scattering highlights discrepancies in Plasmodium multi-aminoacyl-tRNA synthetase complexes.Protein science : a publication of the Protein Society · 2023Article
- Moonlighting translation factors: multifunctionality drives diverse gene regulation.Trends in cell biology · 2022Review
- Proteomics reveal cap-dependent translation inhibitors remodel the translation machinery and translatome.Cell reports · 2021Article
- AIMP3 inhibits cell growth and metastasis of lung adenocarcinoma through activating a miR-96-5p-AIMP3-p53 axis.Journal of cellular and molecular medicine · 2021Article
- 3-Dimensional architecture of the human multi-tRNA synthetase complex.Nucleic acids research · 2020Article
- Aminoacyl-tRNA synthetases.RNA (New York, N.Y.) · 2020Review
- Fission Yeast Asc1 Stabilizes the Interaction between Eukaryotic Initiation Factor 3a and Rps0A/uS2 for Protein Synthesis.Molecular and cellular biology · 2019Article
- Screening of underlying genetic biomarkers for ankylosing spondylitis.Molecular medicine reports · 2019Article
- Evolution of the multi-tRNA synthetase complex and its role in cancer.The Journal of biological chemistry · 2019Review
- AIMP3 Deletion Induces Acute Radiation Syndrome-like Phenotype in Mice.Scientific reports · 2018Article
- AIMP3 depletion causes genome instability and loss of stemness in mouse embryonic stem cells.Cell death & disease · 2018Article
- Biocon's target factory.Nature biotechnology · 2018Article
- Highly chromophoric Cy5-methionine for N-terminal fluorescent tagging of proteins in eukaryotic translation systems.Scientific reports · 2017Article
- Mapping the contact surfaces in the Lamin A:AIMP3 complex by hydrogen/deuterium exchange FT-ICR mass spectrometry.PloS one · 2017Article
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Aminoacyl-tRNA synthetase-interacting multifunctional proteins (AIMPs) are nonenzymatic scaffolding proteins that comprise multisynthetase complex (MSC) with nine aminoacyl-tRNA synthetases in higher eukaryotes. Among the three AIMPs, AIMP3/p18 is strongly anchored to methionyl-tRNA synthetase (MRS) in the MSC. MRS attaches methionine (Met) to initiator tRNA (tRNA(i)(Met)) and plays an important role in translation initiation. It is known that AIMP3 is dispatched to nucleus or nuclear membrane to induce DNA damage response or senescence; however, the role of AIMP3 in translation as a component of MSC and the meaning of its interaction with MRS are still unclear. Herein, we observed that AIMP3 specifically interacted with Met-tRNA(i)(Met)in vitro, while it showed little or reduced interaction with unacylated or lysine-charged tRNA(i)(Met). In addition, AIMP3 discriminates Met-tRNA(i)(Met) from Met-charged elongator tRNA based on filter-binding assay. Pull-down assay revealed that AIMP3 and MRS had noncompetitive interaction with eukaryotic initiation factor 2 (eIF2) γ subunit (eIF2γ), which is in charge of binding with Met-tRNA(i)(Met) for the delivery of Met-tRNA(i)(Met) to ribosome. AIMP3 recruited active eIF2γ to the MRS-AIMP3 complex, and the level of Met-tRNA(i)(Met) bound to eIF2 complex was reduced by AIMP3 knockdown resulting in reduced protein synthesis. All these results suggested the novel function of AIMP3 as a critical mediator of Met-tRNA(i)(Met) transfer from MRS to eIF2 complex for the accurate and efficient translation initiation.
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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.