Component

Human cytosolic threonyl-tRNA synthetase / TARS1

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

6 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. Human cytosolic TARS aminoacylation assays measured threonine loading onto tRNA and competitive inhibition by borrelidin-class compounds.

    Human cytosolic threonyl-tRNA synthetase / TARS1 → Human cytosolic threonyl-tRNA Thr source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Human enzyme biochemistry alongside inhibitor structures and cellular studies.
    limitations
    The charging reaction and extracellular signaling by the enzyme are separate functions.
    nutrient_topic
    L-Threonine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Threonine
    plain_language
    The amino acid must be attached to its matching tRNA before translation.
    primary_references
    Aminoacyl-tRNA synthetase dependent angiogenesis revealed by a bioengineered macrolide inhibitor. · 2015 · https://pubmed.ncbi.nlm.nih.gov/26271225/ · DOI 10.1038/srep13160

    L-Threonine: translation, intestinal barrier, metabolism and cross-nutrient mechanisms (2026-09-19) · lines 58–64

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human enzyme biochemistry alongside inhibitor structures and cellular studies. · source_derived_draft · unverified_draft

    ## l-threonine-tars1-charging The amino acid must be attached to its matching tRNA before translation. Human cytosolic TARS aminoacylation assays measured threonine loading onto tRNA and competitive inhibition by borrelidin-class compounds. Model: Human enzyme biochemistry alongside inhibitor structures and cellular studies. Limitations: The charging reaction and extracellular signaling by the enzyme are separate functions. Evidence access: Primary abstract Aminoacyl-tRNA synthetase dependent angiogenesis revealed by a bioengineered macrolide inhibitor. · 2015 · https://pubmed.ncbi.nlm.nih.gov/26271225/ · DOI 10.1038/srep13160
    Complete structured claim and evidence

  2. Exogenous TARS promoted endothelial migration and angiogenesis in culture and chick chorioallantoic membrane assays.

    Human cytosolic threonyl-tRNA synthetase / TARS1 → Endothelial migration and angiogenesis following extracellular TARS source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Human endothelial assays and chick membrane model.
    limitations
    Enzyme exposure is not amino-acid supplementation; no claim of dietary cancer causation is made.
    nutrient_topic
    L-Threonine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Threonine
    plain_language
    The same enzyme has an extracellular signaling role.
    primary_references
    Secreted Threonyl-tRNA synthetase stimulates endothelial cell migration and angiogenesis. · 2013 · https://pubmed.ncbi.nlm.nih.gov/23425968/ · DOI 10.1038/srep01317

    L-Threonine: translation, intestinal barrier, metabolism and cross-nutrient mechanisms (2026-09-19) · lines 386–392

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human endothelial assays and chick membrane model. · source_derived_draft · unverified_draft

    ## l-threonine-tars1-extracellular The same enzyme has an extracellular signaling role. Exogenous TARS promoted endothelial migration and angiogenesis in culture and chick chorioallantoic membrane assays. Model: Human endothelial assays and chick membrane model. Limitations: Enzyme exposure is not amino-acid supplementation; no claim of dietary cancer causation is made. Evidence access: Primary abstract Secreted Threonyl-tRNA synthetase stimulates endothelial cell migration and angiogenesis. · 2013 · https://pubmed.ncbi.nlm.nih.gov/23425968/ · DOI 10.1038/srep01317
    Complete structured claim and evidence

  3. Human endothelial cells secreted TARS after TNF-alpha or VEGF exposure.

    Human cytosolic threonyl-tRNA synthetase / TARS1 → Human endothelial TNF-alpha or VEGF stimulation source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Human vascular endothelial cell culture.
    limitations
    This is secretion of the enzyme, not secretion of threonine or proof that dietary threonine triggers the process.
    nutrient_topic
    L-Threonine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Threonine
    plain_language
    A protein that loads threonine can also leave the cell under signaling conditions.
    primary_references
    Secreted Threonyl-tRNA synthetase stimulates endothelial cell migration and angiogenesis. · 2013 · https://pubmed.ncbi.nlm.nih.gov/23425968/ · DOI 10.1038/srep01317

    L-Threonine: translation, intestinal barrier, metabolism and cross-nutrient mechanisms (2026-09-19) · lines 378–384

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human vascular endothelial cell culture. · source_derived_draft · unverified_draft

    ## l-threonine-tars1-secretion A protein that loads threonine can also leave the cell under signaling conditions. Human endothelial cells secreted TARS after TNF-alpha or VEGF exposure. Model: Human vascular endothelial cell culture. Limitations: This is secretion of the enzyme, not secretion of threonine or proof that dietary threonine triggers the process. Evidence access: Primary abstract Secreted Threonyl-tRNA synthetase stimulates endothelial cell migration and angiogenesis. · 2013 · https://pubmed.ncbi.nlm.nih.gov/23425968/ · DOI 10.1038/srep01317
    Complete structured claim and evidence

  4. Threonyl-tRNA synthetase interacted with 4EHP and recruited initiation components into a translation-initiation machinery that selected target mRNAs.

    Human cytosolic threonyl-tRNA synthetase / TARS1 → Human eIF4E homologous protein / 4EHP / EIF4E2 source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Biochemical interaction and RNA immunoprecipitation/sequencing analyses in vertebrate models.
    limitations
    This scaffold function is not evidence that adding free threonine increases translation of the same targets.
    nutrient_topic
    L-Threonine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Threonine
    plain_language
    A tRNA-loading enzyme can also help organize translation initiation.
    primary_references
    A threonyl-tRNA synthetase-mediated translation initiation machinery. · 2019 · https://pubmed.ncbi.nlm.nih.gov/30902983/ · DOI 10.1038/s41467-019-09086-0

    L-Threonine: translation, intestinal barrier, metabolism and cross-nutrient mechanisms (2026-09-19) · lines 178–184

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Biochemical interaction and RNA immunoprecipitation/sequencing analyses in vertebrate models. · source_derived_draft · unverified_draft

    ## l-threonine-tars1-translation-scaffold A tRNA-loading enzyme can also help organize translation initiation. Threonyl-tRNA synthetase interacted with 4EHP and recruited initiation components into a translation-initiation machinery that selected target mRNAs. Model: Biochemical interaction and RNA immunoprecipitation/sequencing analyses in vertebrate models. Limitations: This scaffold function is not evidence that adding free threonine increases translation of the same targets. Evidence access: Primary abstract A threonyl-tRNA synthetase-mediated translation initiation machinery. · 2019 · https://pubmed.ncbi.nlm.nih.gov/30902983/ · DOI 10.1038/s41467-019-09086-0
    Complete structured claim and evidence

What acts on it

  1. Borrelidin-class inhibitor toxicity was linked to competition with threonine at TARS, provoking amino-acid-starvation responses and apoptosis in the studied systems.

    Borrelidin → Human cytosolic threonyl-tRNA synthetase / TARS1 source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Enzyme biochemistry, structures, cellular assays and zebrafish work.
    limitations
    Anti-angiogenic action could be separated from toxicity with selected derivatives; these are experimental agents, not routine nutrient interactions.
    nutrient_topic
    L-Threonine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Threonine
    plain_language
    Blocking amino-acid processing can mimic inadequate supply inside a cell.
    primary_references
    Aminoacyl-tRNA synthetase dependent angiogenesis revealed by a bioengineered macrolide inhibitor. · 2015 · https://pubmed.ncbi.nlm.nih.gov/26271225/ · DOI 10.1038/srep13160

    L-Threonine: translation, intestinal barrier, metabolism and cross-nutrient mechanisms (2026-09-19) · lines 394–400

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Enzyme biochemistry, structures, cellular assays and zebrafish work. · source_derived_draft · unverified_draft

    ## l-threonine-borrelidin-competition Blocking amino-acid processing can mimic inadequate supply inside a cell. Borrelidin-class inhibitor toxicity was linked to competition with threonine at TARS, provoking amino-acid-starvation responses and apoptosis in the studied systems. Model: Enzyme biochemistry, structures, cellular assays and zebrafish work. Limitations: Anti-angiogenic action could be separated from toxicity with selected derivatives; these are experimental agents, not routine nutrient interactions. Evidence access: Primary abstract Aminoacyl-tRNA synthetase dependent angiogenesis revealed by a bioengineered macrolide inhibitor. · 2015 · https://pubmed.ncbi.nlm.nih.gov/26271225/ · DOI 10.1038/srep13160
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. Cells lacking TARS2 failed to restore mTORC1 activation in response to threonine repletion; cytosolic TARS was not required for this signaling effect.

    Human mitochondrial threonyl-tRNA synthetase / TARS2 → Threonine-responsive human cellular mTORC1 activation source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    evidence_access
    Primary abstract
    experimental_model
    TARS2 loss and threonine repletion in cultured cells.
    limitations
    This is a signaling endpoint, not a clinical threonine-repletion trial.
    nutrient_topic
    L-Threonine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Threonine
    plain_language
    Restoring the nutrient did not restore the signal when its machinery was missing.
    primary_references
    Mitochondrial Threonyl-tRNA Synthetase TARS2 Is Required for Threonine-Sensitive mTORC1 Activation. · 2021 · https://pubmed.ncbi.nlm.nih.gov/33340489/ · DOI 10.1016/j.molcel.2020.11.036
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    L-Threonine: translation, intestinal barrier, metabolism and cross-nutrient mechanisms (2026-09-19) · lines 106–112

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · TARS2 loss and threonine repletion in cultured cells. · source_derived_draft · unverified_draft

    ## l-threonine-tars2-repletion-failure Restoring the nutrient did not restore the signal when its machinery was missing. Cells lacking TARS2 failed to restore mTORC1 activation in response to threonine repletion; cytosolic TARS was not required for this signaling effect. Model: TARS2 loss and threonine repletion in cultured cells. Limitations: This is a signaling endpoint, not a clinical threonine-repletion trial. Evidence access: Primary abstract Mitochondrial Threonyl-tRNA Synthetase TARS2 Is Required for Threonine-Sensitive mTORC1 Activation. · 2021 · https://pubmed.ncbi.nlm.nih.gov/33340489/ · DOI 10.1016/j.molcel.2020.11.036
    Complete structured claim and evidence

In the sources

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

    This is a research prototype built from draft material. It is not medical advice, and its statements still await verification against the original studies.

    Evidence, AI assistance and curation standards