ArticleMolecular cell2013
Structural switch of lysyl-tRNA synthetase between translation and transcription.
Article in Molecular cell, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 86 papers.
What it found
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Who cites it
86 citing papers in PubMed, 139 citations in OpenAlex.
- Detection and sequencing of ApProceedings of the National Academy of Sciences of the United States of America · 2026Article
- Human aminoacyl-tRNA synthetases as integrators of translation and cell signalling networks.Nature reviews. Molecular cell biology · 2026Review
- Ap4A in Cancer: A Multifaceted Regulator and Emerging Therapeutic Target.Molecules (Basel, Switzerland) · 2025Review
- Lysyl-tRNA synthetase 1 promotes atherogenesis via autophagy-related secretion and inflammation.Scientific reports · 2025Article
- Structural basis for aminoacylation of cellular modified tRNALys3 by human lysyl-tRNA synthetase.Nucleic acids research · 2025Article
- Structural basis for aminoacylation of cellular modified tRNAbioRxiv : the preprint server for biology · 2024Article
- AIMP2 restricts EV71 replication by recruiting SMURF2 to promote the degradation of 3D polymerase.Virologica Sinica · 2024Article
- Protein-Protein Interactions of Seryl-tRNA Synthetases with Emphasis on Human Counterparts and Their Connection to Health and Disease.Life (Basel, Switzerland) · 2024Review
- The MRGPR family of receptors in immunity.Immunity · 2024Review
- Bi-directional regulation of AIMP2 and its splice variant on PARP-1-dependent neuronal cell death; Therapeutic implication for Parkinson's disease.Acta neuropathologica communications · 2024Article
- The mARS complex: a critical mediator of immune regulation and homeostasis.Frontiers in immunology · 2024Review
- Human lysyl-tRNA synthetase phosphorylation promotes HIV-1 proviral DNA transcription.Nucleic acids research · 2023Article
- Domain collapse and active site ablation generate a widespread animal mitochondrial seryl-tRNA synthetase.Nucleic acids research · 2023Article
- Phosphocode-dependent glutamyl-prolyl-tRNA synthetase 1 signaling in immunity, metabolism, and disease.Experimental & molecular medicine · 2023Review
- Role of Nudt2 in Anchorage-Independent Growth and Cell Migration of Human Melanoma.International journal of molecular sciences · 2023Article
- Molecular and Pathological Analyses of IARS1-Deficient Mice: An IARS Disorder Model.International journal of molecular sciences · 2023Article
- Arg-tRNA synthetase links inflammatory metabolism to RNA splicing and nuclear trafficking via SRRM2.Nature cell biology · 2023Article
- Sequential magnesium binding facilitates lysyl-tRNA synthetase to recognize ATP.Biochemistry and biophysics reports · 2023Article
- Recessive aminoacyl-tRNA synthetase disorders: lessons learned fromFrontiers in neuroscience · 2023Review
- Regulatory mechanisms of exopolysaccharide synthesis and biofilm formation in Streptococcus mutans.Journal of oral microbiology · 2023Review
26 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
17 authors at 4 institutions in 3 countries.
Funding
Abstract
Lysyl-tRNA synthetase (LysRS), a component of the translation apparatus, is released from the cytoplasmic multi-tRNA synthetase complex (MSC) to activate the transcription factor MITF in stimulated mast cells through undefined mechanisms. Here we show that Ser207 phosphorylation provokes a new conformer of LysRS that inactivates its translational function but activates its transcriptional function. The crystal structure of an MSC subcomplex established that LysRS is held in the MSC by binding to the N terminus of the scaffold protein p38/AIMP2. Phosphorylation-created steric clashes at the LysRS domain interface disrupt its binding grooves for p38/AIMP2, releasing LysRS and provoking its nuclear translocation. This alteration also exposes the C-terminal domain of LysRS to bind to MITF and triggers LysRS-directed production of the second messenger Ap(4)A that activates MITF. Thus our results establish that a single conformational change triggered by phosphorylation leads to multiple effects driving an exclusive switch of LysRS function from translation to transcription.
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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.