Component

Human cytosolic tyrosyl-tRNA synthetase / YARS1

Context-specific entity; species, compartment and exposure are stated on each claim.

10 recorded relationships. Experimental role, claim status and evidence remain attached to each record.

Read recorded mechanisms Open recursive mind map

How nutrients influence it

Every nutrient with a recorded effect on this component, credited to the nutrient that acted rather than the chapter that recorded it. Open a nutrient to see the findings and the conditions they were measured under.

How nutrients reach it in more than one step

Chains of two or more recorded steps that end here, grouped by the nutrient they start from. Each step is a separate finding, so a chain is a route a mechanism could take, not proof that it does.

Tracing routes…

What it does

Every recorded relationship this component is part of, grouped by its role. Plain wording comes first; the technical statement follows.

Recorded relationships

What it acts on

  1. Silencing TyrRS abolished the one-hour NAD increase induced by low-dose resveratrol in human HeLa cells.

    Human cytosolic tyrosyl-tRNA synthetase / YARS1 → NAD content in human HeLa cells source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    evidence_access
    Primary full text
    experimental_model
    siRNA experiments; 5 micromolar resveratrol.
    limitations
    Cell-model dependency, not a dietary resveratrol-deficiency state.
    nutrient_topic
    Resveratrol collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Resveratrol
    plain_language
    Removing a signaling component prevented the rebound.
    primary_references
    A human tRNA synthetase is a potent PARP1-activating effector target for resveratrol. · 2015 · https://pubmed.ncbi.nlm.nih.gov/25533949/ · DOI 10.1038/nature14028
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    Resveratrol: metabolites, target selectivity and cross-nutrient mechanisms (2026-09-19) · lines 318–324

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · siRNA experiments; 5 micromolar resveratrol. · source_derived_draft · unverified_draft

    ## resveratrol-tyrrs-loss Removing a signaling component prevented the rebound. Silencing TyrRS abolished the one-hour NAD increase induced by low-dose resveratrol in human HeLa cells. Model: siRNA experiments; 5 micromolar resveratrol. Limitations: Cell-model dependency, not a dietary resveratrol-deficiency state. Evidence access: Primary full text A human tRNA synthetase is a potent PARP1-activating effector target for resveratrol. · 2015 · https://pubmed.ncbi.nlm.nih.gov/25533949/ · DOI 10.1038/nature14028
    Complete structured claim and evidence

  2. In the resveratrol study, human TyrRS stimulated NAD-dependent PARP1 auto-poly-ADP-ribosylation in biochemical experiments.

    Human cytosolic tyrosyl-tRNA synthetase / YARS1 → Human PARP1 source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary full text
    experimental_model
    Purified-protein interaction/activation assays.
    limitations
    Greater PARylation need not imply greater net NAD stores.
    nutrient_topic
    Resveratrol collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Resveratrol
    plain_language
    This signaling step consumes a niacin-derived cofactor.
    primary_references
    A human tRNA synthetase is a potent PARP1-activating effector target for resveratrol. · 2015 · https://pubmed.ncbi.nlm.nih.gov/25533949/ · DOI 10.1038/nature14028

    Resveratrol: metabolites, target selectivity and cross-nutrient mechanisms (2026-09-19) · lines 302–308

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Purified-protein interaction/activation assays. · source_derived_draft · unverified_draft

    ## resveratrol-tyrrs-parp This signaling step consumes a niacin-derived cofactor. In the resveratrol study, human TyrRS stimulated NAD-dependent PARP1 auto-poly-ADP-ribosylation in biochemical experiments. Model: Purified-protein interaction/activation assays. Limitations: Greater PARylation need not imply greater net NAD stores. Evidence access: Primary full text A human tRNA synthetase is a potent PARP1-activating effector target for resveratrol. · 2015 · https://pubmed.ncbi.nlm.nih.gov/25533949/ · DOI 10.1038/nature14028
    Complete structured claim and evidence

  3. Human YARS1 ligates tyrosine to its cognate tRNA; the study separately examined the extracellular functions of this protein.

    Human cytosolic tyrosyl-tRNA synthetase / YARS1 → Human cytosolic Tyr-tRNA Tyr source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary full text; reaction description and experimental methods
    experimental_model
    Primary-paper description of YARS1 chemistry and human cellular/protein experiments.
    limitations
    The translation role is biochemical background in this paper; the main experiments concern extracellular signaling.
    nutrient_topic
    L-Tyrosine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Tyrosine
    plain_language
    Tyrosine must be loaded onto tRNA to enter a growing protein.
    primary_references
    Moonlighting matrix metalloproteinase substrates: Enhancement of proinflammatory functions of extracellular tyrosyl-tRNA synthetase upon cleavage. · 2020 · https://pubmed.ncbi.nlm.nih.gov/31771979/ · DOI 10.1074/jbc.RA119.010486

    L-Tyrosine: catecholamines, thyroid chemistry, pigment, metabolism and cross-nutrient mechanisms (2026-09-19) · lines 68–74

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Primary-paper description of YARS1 chemistry and human cellular/protein experiments. · source_derived_draft · unverified_draft

    ## l-tyrosine-yars1-charging Tyrosine must be loaded onto tRNA to enter a growing protein. Human YARS1 ligates tyrosine to its cognate tRNA; the study separately examined the extracellular functions of this protein. Model: Primary-paper description of YARS1 chemistry and human cellular/protein experiments. Limitations: The translation role is biochemical background in this paper; the main experiments concern extracellular signaling. Evidence access: Primary full text; reaction description and experimental methods Moonlighting matrix metalloproteinase substrates: Enhancement of proinflammatory functions of extracellular tyrosyl-tRNA synthetase upon cleavage. · 2020 · https://pubmed.ncbi.nlm.nih.gov/31771979/ · DOI 10.1074/jbc.RA119.010486
    Complete structured claim and evidence

  4. Extracellular YARS1 activated TLR2 signaling and inflammatory mediator release in human monocyte/macrophage preparations.

    Human cytosolic tyrosyl-tRNA synthetase / YARS1 → Human Toll-like receptor 2 / TLR2 source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary full text and abstract
    experimental_model
    THP1 and peripheral-blood-derived macrophages; purified protein exposure.
    limitations
    This differs from intracellular charging and from assays of individual fragments.
    nutrient_topic
    L-Tyrosine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Tyrosine
    plain_language
    A protein used for translation also signals outside cells.
    primary_references
    Moonlighting matrix metalloproteinase substrates: Enhancement of proinflammatory functions of extracellular tyrosyl-tRNA synthetase upon cleavage. · 2020 · https://pubmed.ncbi.nlm.nih.gov/31771979/ · DOI 10.1074/jbc.RA119.010486

    L-Tyrosine: catecholamines, thyroid chemistry, pigment, metabolism and cross-nutrient mechanisms (2026-09-19) · lines 108–114

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · THP1 and peripheral-blood-derived macrophages; purified protein exposure. · source_derived_draft · unverified_draft

    ## l-tyrosine-yrs-tlr2 A protein used for translation also signals outside cells. Extracellular YARS1 activated TLR2 signaling and inflammatory mediator release in human monocyte/macrophage preparations. Model: THP1 and peripheral-blood-derived macrophages; purified protein exposure. Limitations: This differs from intracellular charging and from assays of individual fragments. Evidence access: Primary full text and abstract Moonlighting matrix metalloproteinase substrates: Enhancement of proinflammatory functions of extracellular tyrosyl-tRNA synthetase upon cleavage. · 2020 · https://pubmed.ncbi.nlm.nih.gov/31771979/ · DOI 10.1074/jbc.RA119.010486
    Complete structured claim and evidence

What acts on it

  1. Resveratrol occupied the tyrosine active site in human TyrRS co-crystals and inhibited amino-acid activation with reported Ki 22 micromolar.

    Resveratrol → Human cytosolic tyrosyl-tRNA synthetase / YARS1 source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary full text
    experimental_model
    Purified human enzyme and structure.
    limitations
    The bound ligand adopts a cis conformation; the authors propose conformational accommodation from predominantly trans solution. This is not proof of physiological bulk photoisomerization.
    nutrient_topic
    Resveratrol collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Resveratrol
    plain_language
    A protein that normally charges tyrosine tRNA also senses this compound.
    primary_references
    A human tRNA synthetase is a potent PARP1-activating effector target for resveratrol. · 2015 · https://pubmed.ncbi.nlm.nih.gov/25533949/ · DOI 10.1038/nature14028

    Resveratrol: metabolites, target selectivity and cross-nutrient mechanisms (2026-09-19) · lines 286–292

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Purified human enzyme and structure. · source_derived_draft · unverified_draft

    ## resveratrol-tyrrs-binding A protein that normally charges tyrosine tRNA also senses this compound. Resveratrol occupied the tyrosine active site in human TyrRS co-crystals and inhibited amino-acid activation with reported Ki 22 micromolar. Model: Purified human enzyme and structure. Limitations: The bound ligand adopts a cis conformation; the authors propose conformational accommodation from predominantly trans solution. This is not proof of physiological bulk photoisomerization. Evidence access: Primary full text A human tRNA synthetase is a potent PARP1-activating effector target for resveratrol. · 2015 · https://pubmed.ncbi.nlm.nih.gov/25533949/ · DOI 10.1038/nature14028
    Complete structured claim and evidence

  2. Resveratrol promoted endogenous TyrRS nuclear translocation in human HeLa cells, coincident with PARP1 auto-PARylation.

    Resveratrol → Human cytosolic tyrosyl-tRNA synthetase / YARS1 source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary full text
    experimental_model
    HeLa time-course and purified interaction experiments.
    limitations
    Compartment change is not general inhibition of protein synthesis in humans.
    nutrient_topic
    Resveratrol collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Resveratrol
    plain_language
    An amino-acid enzyme moves into a stress-signaling role.
    primary_references
    A human tRNA synthetase is a potent PARP1-activating effector target for resveratrol. · 2015 · https://pubmed.ncbi.nlm.nih.gov/25533949/ · DOI 10.1038/nature14028

    Resveratrol: metabolites, target selectivity and cross-nutrient mechanisms (2026-09-19) · lines 294–300

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · HeLa time-course and purified interaction experiments. · source_derived_draft · unverified_draft

    ## resveratrol-tyrrs-nucleus An amino-acid enzyme moves into a stress-signaling role. Resveratrol promoted endogenous TyrRS nuclear translocation in human HeLa cells, coincident with PARP1 auto-PARylation. Model: HeLa time-course and purified interaction experiments. Limitations: Compartment change is not general inhibition of protein synthesis in humans. Evidence access: Primary full text A human tRNA synthetase is a potent PARP1-activating effector target for resveratrol. · 2015 · https://pubmed.ncbi.nlm.nih.gov/25533949/ · DOI 10.1038/nature14028
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. At 0.5 millimolar in the substrate preincubation assay, tyrosine inhibited MMP8 cleavage of YARS1 but did not inhibit MMP7 cleavage.

    L-Tyrosine → Human MMP8 cleavage of YARS1 source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary full text; substrate/product cleavage methods and results
    experimental_model
    30-minute substrate preincubation at 22 degrees C; subsequent recombinant-enzyme cleavage assay.
    limitations
    This is not demonstrated inhibition of MMP8 generally or a clinical anti-inflammatory effect.
    nutrient_topic
    L-Tyrosine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Tyrosine
    plain_language
    The amino acid can alter how one protease handles its loading enzyme.
    primary_references
    Moonlighting matrix metalloproteinase substrates: Enhancement of proinflammatory functions of extracellular tyrosyl-tRNA synthetase upon cleavage. · 2020 · https://pubmed.ncbi.nlm.nih.gov/31771979/ · DOI 10.1074/jbc.RA119.010486

    L-Tyrosine: catecholamines, thyroid chemistry, pigment, metabolism and cross-nutrient mechanisms (2026-09-19) · lines 124–130

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · 30-minute substrate preincubation at 22 degrees C; subsequent recombinant-enzyme cleavage assay. · source_derived_draft · unverified_draft

    ## l-tyrosine-tyrosine-cleavage The amino acid can alter how one protease handles its loading enzyme. At 0.5 millimolar in the substrate preincubation assay, tyrosine inhibited MMP8 cleavage of YARS1 but did not inhibit MMP7 cleavage. Model: 30-minute substrate preincubation at 22 degrees C; subsequent recombinant-enzyme cleavage assay. Limitations: This is not demonstrated inhibition of MMP8 generally or a clinical anti-inflammatory effect. Evidence access: Primary full text; substrate/product cleavage methods and results Moonlighting matrix metalloproteinase substrates: Enhancement of proinflammatory functions of extracellular tyrosyl-tRNA synthetase upon cleavage. · 2020 · https://pubmed.ncbi.nlm.nih.gov/31771979/ · DOI 10.1074/jbc.RA119.010486
    Complete structured claim and evidence

  2. A heptapeptide from the human YARS1 C-domain induced chemotaxis of mononuclear phagocytes and polymorphonuclear leukocytes.

    Human YARS1 C-terminal EMAPII-like fragment → Human leukocyte chemotaxis induced by YARS1 fragments source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    C-domain peptide assays and sequence-specific controls.
    limitations
    Other proteins with similar motifs were inactive in these assays; sequence similarity alone is insufficient.
    nutrient_topic
    L-Tyrosine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Tyrosine
    plain_language
    A different part of the same protein has another signaling activity.
    primary_references
    Highly differentiated motifs responsible for two cytokine activities of a split human tRNA synthetase. · 1999 · https://pubmed.ncbi.nlm.nih.gov/10438485/ · DOI 10.1074/jbc.274.33.23155

    L-Tyrosine: catecholamines, thyroid chemistry, pigment, metabolism and cross-nutrient mechanisms (2026-09-19) · lines 100–106

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · C-domain peptide assays and sequence-specific controls. · source_derived_draft · unverified_draft

    ## l-tyrosine-yars-c-domain A different part of the same protein has another signaling activity. A heptapeptide from the human YARS1 C-domain induced chemotaxis of mononuclear phagocytes and polymorphonuclear leukocytes. Model: C-domain peptide assays and sequence-specific controls. Limitations: Other proteins with similar motifs were inactive in these assays; sequence similarity alone is insufficient. Evidence access: Primary abstract Highly differentiated motifs responsible for two cytokine activities of a split human tRNA synthetase. · 1999 · https://pubmed.ncbi.nlm.nih.gov/10438485/ · DOI 10.1074/jbc.274.33.23155
    Complete structured claim and evidence

  3. The human YARS1 N-terminal fragment exhibited IL-8-like activity dependent on its differentiated ELR motif.

    Human YARS1 N-terminal cytokine fragment → Human leukocyte chemotaxis induced by YARS1 fragments source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Human recombinant fragments and motif comparison with lower-eukaryote TyrRS.
    limitations
    This fragment is not free tyrosine, and its activity is not a supplement effect.
    nutrient_topic
    L-Tyrosine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Tyrosine
    plain_language
    Cutting a protein can expose a signaling function.
    primary_references
    Highly differentiated motifs responsible for two cytokine activities of a split human tRNA synthetase. · 1999 · https://pubmed.ncbi.nlm.nih.gov/10438485/ · DOI 10.1074/jbc.274.33.23155

    L-Tyrosine: catecholamines, thyroid chemistry, pigment, metabolism and cross-nutrient mechanisms (2026-09-19) · lines 92–98

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human recombinant fragments and motif comparison with lower-eukaryote TyrRS. · source_derived_draft · unverified_draft

    ## l-tyrosine-yars-fragment Cutting a protein can expose a signaling function. The human YARS1 N-terminal fragment exhibited IL-8-like activity dependent on its differentiated ELR motif. Model: Human recombinant fragments and motif comparison with lower-eukaryote TyrRS. Limitations: This fragment is not free tyrosine, and its activity is not a supplement effect. Evidence access: Primary abstract Highly differentiated motifs responsible for two cytokine activities of a split human tRNA synthetase. · 1999 · https://pubmed.ncbi.nlm.nih.gov/10438485/ · DOI 10.1074/jbc.274.33.23155
    Complete structured claim and evidence

  4. MMP cleavage of YARS1 increased TLR2 signaling, TNF secretion and chemotaxis relative to unprocessed YARS1.

    Human matrix metalloproteinase 8 / MMP8 → Human YARS1 proteolysis-dependent inflammatory signaling source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary full text and abstract
    experimental_model
    Protein cleavage and macrophage assays; MMP7 and MMP8 among tested enzymes.
    limitations
    A proposed feed-forward inflammatory loop still requires in vivo testing.
    nutrient_topic
    L-Tyrosine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Tyrosine
    plain_language
    Protease activity changes the strength of an extracellular signal.
    primary_references
    Moonlighting matrix metalloproteinase substrates: Enhancement of proinflammatory functions of extracellular tyrosyl-tRNA synthetase upon cleavage. · 2020 · https://pubmed.ncbi.nlm.nih.gov/31771979/ · DOI 10.1074/jbc.RA119.010486

    L-Tyrosine: catecholamines, thyroid chemistry, pigment, metabolism and cross-nutrient mechanisms (2026-09-19) · lines 116–122

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Protein cleavage and macrophage assays; MMP7 and MMP8 among tested enzymes. · source_derived_draft · unverified_draft

    ## l-tyrosine-yrs-proteolysis Protease activity changes the strength of an extracellular signal. MMP cleavage of YARS1 increased TLR2 signaling, TNF secretion and chemotaxis relative to unprocessed YARS1. Model: Protein cleavage and macrophage assays; MMP7 and MMP8 among tested enzymes. Limitations: A proposed feed-forward inflammatory loop still requires in vivo testing. Evidence access: Primary full text and abstract Moonlighting matrix metalloproteinase substrates: Enhancement of proinflammatory functions of extracellular tyrosyl-tRNA synthetase upon cleavage. · 2020 · https://pubmed.ncbi.nlm.nih.gov/31771979/ · DOI 10.1074/jbc.RA119.010486
    Complete structured claim and evidence

In the sources

Preserved passages that mention this component, quoted exactly. Open one to read it in context.

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