ArticleNature2015
A human tRNA synthetase is a potent PARP1-activating effector target for resveratrol.
Article in Nature, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 75 papers.
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Who cites it
75 citing papers in PubMed, 144 citations in OpenAlex.
- The TyrRS cascade: circadian gating of neuronal DNA repair and its collapse in aging.GeroScience · 2026Review
- Human aminoacyl-tRNA synthetases as integrators of translation and cell signalling networks.Nature reviews. Molecular cell biology · 2026Review
- Targeting tRNA-dependent tyrosine usage unveils a metabolic vulnerability in hepatocellular carcinoma.Nature communications · 2026Article
- Article
- An mRNA vaccine induces antimycobacterial immunity by activating DNA damage repair and autophagy.Molecular therapy. Nucleic acids · 2025Article
- Insights into Molecular Interactions and Biological Effect of Natural Stilbenoids at the TRPA1 Ion Channel.ChemMedChem · 2025Article
- Potential Transformation of Food Resveratrol: Mechanisms and Biological Impact.Molecules (Basel, Switzerland) · 2025Review
- ISR Modulators in Neurological Diseases.Current neuropharmacology · 2025Review
- Resveratrol Inhibits Nucleosome Binding and Catalytic Activity of PARP1.Biomolecules · 2024Article
- AKT-dependent nuclear localization of EPRS1 activates PARP1 in breast cancer cells.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Competitive Inhibition of Okanin againstInternational journal of molecular sciences · 2024Article
- Nuclear translocation of an aminoacyl-tRNA synthetase may mediate a chronic "integrated stress response".Cell reports · 2023Article
- Low-Dose Trans-Resveratrol Ameliorates Diabetes-Induced Retinal Ganglion Cell Degeneration via TyrRS/c-Jun Pathway.Investigative ophthalmology & visual science · 2023Article
- Resveratrol Protects against Skin Inflammation through Inhibition of Mast Cell, Sphingosine Kinase-1, Stat3 and NF-κB p65 Signaling Activation in Mice.International journal of molecular sciences · 2023Article
- Arg-tRNA synthetase links inflammatory metabolism to RNA splicing and nuclear trafficking via SRRM2.Nature cell biology · 2023Article
- Cytoplasmic isoleucyl tRNA synthetase as an attractive multistage antimalarial drug target.Science translational medicine · 2023Article
- Gut microbial characteristical comparison reveals potential anti-aging function ofFrontiers in endocrinology · 2023Article
- A neuronal action of sirtuin 1 suppresses bone mass in young and aging mice.The Journal of clinical investigation · 2022Article
- Interactive Effects of Copper and Functional Substances in Wine on Alcoholic Hepatic Injury in Mice.Foods (Basel, Switzerland) · 2022Article
- Modulation of Excitatory Synaptic Transmission During Cannabinoid Receptor Activation.Cellular and molecular neurobiology · 2022Article
15 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
2 authors at 2 institutions in 1 country.
Funding
Abstract
Resveratrol is reported to extend lifespan and provide cardio-neuro-protective, anti-diabetic, and anti-cancer effects by initiating a stress response that induces survival genes. Because human tyrosyl transfer-RNA (tRNA) synthetase (TyrRS) translocates to the nucleus under stress conditions, we considered the possibility that the tyrosine-like phenolic ring of resveratrol might fit into the active site pocket to effect a nuclear role. Here we present a 2.1 Å co-crystal structure of resveratrol bound to the active site of TyrRS. Resveratrol nullifies the catalytic activity and redirects TyrRS to a nuclear function, stimulating NAD(+)-dependent auto-poly-ADP-ribosylation of poly(ADP-ribose) polymerase 1 (PARP1). Downstream activation of key stress signalling pathways are causally connected to TyrRS-PARP1-NAD(+) collaboration. This collaboration is also demonstrated in the mouse, and is specifically blocked in vivo by a resveratrol-displacing tyrosyl adenylate analogue. In contrast to functionally diverse tRNA synthetase catalytic nulls created by alternative splicing events that ablate active sites, here a non-spliced TyrRS catalytic null reveals a new PARP1- and NAD(+)-dependent dimension to the physiological mechanism of resveratrol.
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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.