Component

Human threonylcarbamoyladenylate synthase / YRDC

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

7 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. Cytosolic t6A formation uses sequential YRDC and OSGEP activities, with OSGEP operating within the KEOPS complex.

    Human threonylcarbamoyladenylate synthase / YRDC → Human KEOPS catalytic subunit / OSGEP source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Primary human genetics and structural study of the t6A pathway.
    limitations
    OSGEP and mitochondrial OSGEPL1 are distinct proteins; threonyl-tRNA loading is a separate reaction.
    nutrient_topic
    L-Threonine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Threonine
    plain_language
    The cytosol uses a different downstream machine from the mitochondrial pathway.
    primary_references
    Defects in t6A tRNA modification due to GON7 and YRDC mutations lead to Galloway-Mowat syndrome. · 2019 · https://pubmed.ncbi.nlm.nih.gov/31481669/ · DOI 10.1038/s41467-019-11951-x

    L-Threonine: translation, intestinal barrier, metabolism and cross-nutrient mechanisms (2026-09-19) · lines 442–448

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Primary human genetics and structural study of the t6A pathway. · source_derived_draft · unverified_draft

    ## l-threonine-cytosolic-keops The cytosol uses a different downstream machine from the mitochondrial pathway. Cytosolic t6A formation uses sequential YRDC and OSGEP activities, with OSGEP operating within the KEOPS complex. Model: Primary human genetics and structural study of the t6A pathway. Limitations: OSGEP and mitochondrial OSGEPL1 are distinct proteins; threonyl-tRNA loading is a separate reaction. Evidence access: Primary abstract Defects in t6A tRNA modification due to GON7 and YRDC mutations lead to Galloway-Mowat syndrome. · 2019 · https://pubmed.ncbi.nlm.nih.gov/31481669/ · DOI 10.1038/s41467-019-11951-x
    Complete structured claim and evidence

  2. The t6A pathway first forms threonylcarbamoyladenylate from threonine, bicarbonate and ATP; OSGEPL1 then transfers the threonylcarbamoyl group to mitochondrial tRNA A37.

    Human threonylcarbamoyladenylate synthase / YRDC → L-Threonylcarbamoyladenylate / TC-AMP source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract and accessible primary-paper pathway description
    experimental_model
    Primary paper pathway description supporting human mitochondrial experiments.
    limitations
    The reaction sequence is described in the primary paper introduction; the 2024 study primarily tests loss of the downstream enzyme.
    nutrient_topic
    L-Threonine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Threonine
    plain_language
    An activated intermediate links nutrient supply to an RNA modification.
    primary_references
    Multifaceted roles of t6A biogenesis in efficiency and fidelity of mitochondrial gene expression. · 2024 · https://pubmed.ncbi.nlm.nih.gov/38227555/ · DOI 10.1093/nar/gkae013

    L-Threonine: translation, intestinal barrier, metabolism and cross-nutrient mechanisms (2026-09-19) · lines 130–136

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Primary paper pathway description supporting human mitochondrial experiments. · source_derived_draft · unverified_draft

    ## l-threonine-trna-intermediate An activated intermediate links nutrient supply to an RNA modification. The t6A pathway first forms threonylcarbamoyladenylate from threonine, bicarbonate and ATP; OSGEPL1 then transfers the threonylcarbamoyl group to mitochondrial tRNA A37. Model: Primary paper pathway description supporting human mitochondrial experiments. Limitations: The reaction sequence is described in the primary paper introduction; the 2024 study primarily tests loss of the downstream enzyme. Evidence access: Primary abstract and accessible primary-paper pathway description Multifaceted roles of t6A biogenesis in efficiency and fidelity of mitochondrial gene expression. · 2024 · https://pubmed.ncbi.nlm.nih.gov/38227555/ · DOI 10.1093/nar/gkae013
    Complete structured claim and evidence

  3. Human YRDC and OSGEPL1 supported mitochondrial t6A37 formation using L-threonine, ATP and CO2/bicarbonate as substrates.

    Human threonylcarbamoyladenylate synthase / YRDC → Human mitochondrial tRNA threonylcarbamoyltransferase / OSGEPL1 source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Human mitochondrial tRNA-modification reconstitution and cellular experiments.
    limitations
    The mark occurs on multiple tRNAs; it is not restricted to the tRNA that carries threonine.
    nutrient_topic
    L-Threonine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Threonine
    plain_language
    Threonine helps make a decoding mark on tRNA, separate from being loaded for protein synthesis.
    primary_references
    CO2-sensitive tRNA modification associated with human mitochondrial disease. · 2018 · https://pubmed.ncbi.nlm.nih.gov/29760464/ · DOI 10.1038/s41467-018-04250-4

    L-Threonine: translation, intestinal barrier, metabolism and cross-nutrient mechanisms (2026-09-19) · lines 122–128

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human mitochondrial tRNA-modification reconstitution and cellular experiments. · source_derived_draft · unverified_draft

    ## l-threonine-trna-mark-substrates Threonine helps make a decoding mark on tRNA, separate from being loaded for protein synthesis. Human YRDC and OSGEPL1 supported mitochondrial t6A37 formation using L-threonine, ATP and CO2/bicarbonate as substrates. Model: Human mitochondrial tRNA-modification reconstitution and cellular experiments. Limitations: The mark occurs on multiple tRNAs; it is not restricted to the tRNA that carries threonine. Evidence access: Primary abstract CO2-sensitive tRNA modification associated with human mitochondrial disease. · 2018 · https://pubmed.ncbi.nlm.nih.gov/29760464/ · DOI 10.1038/s41467-018-04250-4
    Complete structured claim and evidence

  4. Targeting YRDC reduced t6A, translation and tumor growth in glioblastoma stem-cell cultures and in vivo tumor models.

    Human threonylcarbamoyladenylate synthase / YRDC → Human glioblastoma stem-cell t6A and translation source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    evidence_access
    Primary abstract
    experimental_model
    CRISPR screen, cultured glioblastoma stem cells and xenografts.
    limitations
    Genetic targeting of YRDC is distinct from nutritional restriction and from a demonstrated human cancer treatment.
    nutrient_topic
    L-Threonine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Threonine
    plain_language
    A tumor model depended on the machinery that uses threonine to modify tRNA.
    primary_references
    Threonine fuels glioblastoma through YRDC-mediated codon-biased translational reprogramming. · 2024 · https://pubmed.ncbi.nlm.nih.gov/38519786/ · DOI 10.1038/s43018-024-00748-7
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    L-Threonine: translation, intestinal barrier, metabolism and cross-nutrient mechanisms (2026-09-19) · lines 362–368

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · CRISPR screen, cultured glioblastoma stem cells and xenografts. · source_derived_draft · unverified_draft

    ## l-threonine-yrdc-glioblastoma A tumor model depended on the machinery that uses threonine to modify tRNA. Targeting YRDC reduced t6A, translation and tumor growth in glioblastoma stem-cell cultures and in vivo tumor models. Model: CRISPR screen, cultured glioblastoma stem cells and xenografts. Limitations: Genetic targeting of YRDC is distinct from nutritional restriction and from a demonstrated human cancer treatment. Evidence access: Primary abstract Threonine fuels glioblastoma through YRDC-mediated codon-biased translational reprogramming. · 2024 · https://pubmed.ncbi.nlm.nih.gov/38519786/ · DOI 10.1038/s43018-024-00748-7
    Complete structured claim and evidence

  5. Inherited YRDC mutations were associated with severe Galloway–Mowat syndrome, linking t6A machinery impairment with microcephaly and early-onset nephrotic disease.

    Human threonylcarbamoyladenylate synthase / YRDC → YRDC-associated Galloway–Mowat syndrome source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    evidence_access
    Primary abstract
    experimental_model
    Human genetic disease study with functional analyses; GON7-associated cases were milder in the reported series.
    limitations
    This is an inherited machinery disorder, not demonstrated dietary threonine deficiency or a proven supplementation-responsive syndrome.
    nutrient_topic
    L-Threonine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Threonine
    plain_language
    A threonine-using RNA pathway matters in human brain and kidney development.
    primary_references
    Defects in t6A tRNA modification due to GON7 and YRDC mutations lead to Galloway-Mowat syndrome. · 2019 · https://pubmed.ncbi.nlm.nih.gov/31481669/ · DOI 10.1038/s41467-019-11951-x
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    L-Threonine: translation, intestinal barrier, metabolism and cross-nutrient mechanisms (2026-09-19) · lines 458–464

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human genetic disease study with functional analyses; GON7-associated cases were milder in the reported series. · source_derived_draft · unverified_draft

    ## l-threonine-yrdc-inherited-disease A threonine-using RNA pathway matters in human brain and kidney development. Inherited YRDC mutations were associated with severe Galloway–Mowat syndrome, linking t6A machinery impairment with microcephaly and early-onset nephrotic disease. Model: Human genetic disease study with functional analyses; GON7-associated cases were milder in the reported series. Limitations: This is an inherited machinery disorder, not demonstrated dietary threonine deficiency or a proven supplementation-responsive syndrome. Evidence access: Primary abstract Defects in t6A tRNA modification due to GON7 and YRDC mutations lead to Galloway-Mowat syndrome. · 2019 · https://pubmed.ncbi.nlm.nih.gov/31481669/ · DOI 10.1038/s41467-019-11951-x
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. The measured bicarbonate/CO2 Km for t6A37 formation was 31 millimolar; human cells cultured without bicarbonate had less t6A37 in mitochondrial tRNAs.

    Bicarbonate ion → tRNA-bound N6-threonylcarbamoyladenosine / t6A37 source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Reconstituted enzyme kinetics and bicarbonate-deprived human cell culture.
    limitations
    The culture manipulation is not a bicarbonate supplementation trial or a clinical intracellular threshold.
    nutrient_topic
    L-Threonine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Threonine
    plain_language
    An additional substrate can limit the threonine-dependent reaction.
    primary_references
    CO2-sensitive tRNA modification associated with human mitochondrial disease. · 2018 · https://pubmed.ncbi.nlm.nih.gov/29760464/ · DOI 10.1038/s41467-018-04250-4

    L-Threonine: translation, intestinal barrier, metabolism and cross-nutrient mechanisms (2026-09-19) · lines 138–144

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Reconstituted enzyme kinetics and bicarbonate-deprived human cell culture. · source_derived_draft · unverified_draft

    ## l-threonine-bicarbonate-limitation An additional substrate can limit the threonine-dependent reaction. The measured bicarbonate/CO2 Km for t6A37 formation was 31 millimolar; human cells cultured without bicarbonate had less t6A37 in mitochondrial tRNAs. Model: Reconstituted enzyme kinetics and bicarbonate-deprived human cell culture. Limitations: The culture manipulation is not a bicarbonate supplementation trial or a clinical intracellular threshold. Evidence access: Primary abstract CO2-sensitive tRNA modification associated with human mitochondrial disease. · 2018 · https://pubmed.ncbi.nlm.nih.gov/29760464/ · DOI 10.1038/s41467-018-04250-4
    Complete structured claim and evidence

  2. Dietary threonine restriction reduced tumor t6A and slowed glioblastoma xenograft growth, augmenting tested chemotherapy and anti-mitotic therapy.

    L-Threonine → Glioblastoma xenograft t6A and growth in mice source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    nutrient_deficiency Imported condition classification; unverified.
    evidence_access
    Primary abstract
    experimental_model
    Mouse xenografts linked to human glioblastoma stem-cell experiments.
    limitations
    This study does not establish a safe or effective threonine-restricted diet for patients. Exact dietary protocol and drug schedules require full-text clinical translation review.
    nutrient_topic
    L-Threonine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Threonine
    plain_language
    Tumor dependency led to an experimental dietary intervention in animals.
    primary_references
    Threonine fuels glioblastoma through YRDC-mediated codon-biased translational reprogramming. · 2024 · https://pubmed.ncbi.nlm.nih.gov/38519786/ · DOI 10.1038/s43018-024-00748-7
    trigger_kind
    nutrient_deficiency Imported condition classification; unverified.

    L-Threonine: translation, intestinal barrier, metabolism and cross-nutrient mechanisms (2026-09-19) · lines 370–376

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Mouse xenografts linked to human glioblastoma stem-cell experiments. · source_derived_draft · unverified_draft

    ## l-threonine-tumor-threonine-restriction Tumor dependency led to an experimental dietary intervention in animals. Dietary threonine restriction reduced tumor t6A and slowed glioblastoma xenograft growth, augmenting tested chemotherapy and anti-mitotic therapy. Model: Mouse xenografts linked to human glioblastoma stem-cell experiments. Limitations: This study does not establish a safe or effective threonine-restricted diet for patients. Exact dietary protocol and drug schedules require full-text clinical translation review. Evidence access: Primary abstract Threonine fuels glioblastoma through YRDC-mediated codon-biased translational reprogramming. · 2024 · https://pubmed.ncbi.nlm.nih.gov/38519786/ · DOI 10.1038/s43018-024-00748-7
    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.

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