Component

Human RagA GTPase / RRAGA

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

2 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

Where it participates (unsigned role)

  1. TARS2 interacted with inactive Rag complexes, especially GTP-bound RagC, and promoted RagA GTP loading.

    Human mitochondrial threonyl-tRNA synthetase / TARS2 → Human RagA GTP loading source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Cellular interaction and mTORC1 signaling experiments.
    limitations
    GTP-bound RagC here belongs to the inactive Rag configuration; GTP status has different implications for RagA and RagC.
    nutrient_topic
    L-Threonine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Threonine
    plain_language
    A threonine-processing protein also links nutrient availability to a growth-control switch.
    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

    L-Threonine: translation, intestinal barrier, metabolism and cross-nutrient mechanisms (2026-09-19) · lines 98–104

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Cellular interaction and mTORC1 signaling experiments. · source_derived_draft · unverified_draft

    ## l-threonine-tars2-rag A threonine-processing protein also links nutrient availability to a growth-control switch. TARS2 interacted with inactive Rag complexes, especially GTP-bound RagC, and promoted RagA GTP loading. Model: Cellular interaction and mTORC1 signaling experiments. Limitations: GTP-bound RagC here belongs to the inactive Rag configuration; GTP status has different implications for RagA and RagC. 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

  2. Disease-associated variants within TARS2 residues 301–381 reduced Rag binding in vitro; the associated mTORC1 mechanism was also investigated in zebrafish.

    Human mitochondrial threonyl-tRNA synthetase / TARS2 → Human TARS2 binding to Rag GTPases source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    evidence_access
    Primary abstract
    experimental_model
    18 newly reported individuals from 15 families, prior cases reviewed, in vitro assays and zebrafish modeling.
    limitations
    Likely mechanistic contribution, not proof that this pathway explains every patient feature.
    nutrient_topic
    L-Threonine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Threonine
    plain_language
    Some variants can affect signaling as well as the usual translation function.
    primary_references
    Clinical, neuroradiological, and molecular characterization of mitochondrial threonyl-tRNA-synthetase (TARS2)-related disorder. · 2023 · https://pubmed.ncbi.nlm.nih.gov/37454282/ · DOI 10.1016/j.gim.2023.100938
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    L-Threonine: translation, intestinal barrier, metabolism and cross-nutrient mechanisms (2026-09-19) · lines 114–120

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · 18 newly reported individuals from 15 families, prior cases reviewed, in vitro assays and zebrafish modeling. · source_derived_draft · unverified_draft

    ## l-threonine-tars2-rag-variants Some variants can affect signaling as well as the usual translation function. Disease-associated variants within TARS2 residues 301–381 reduced Rag binding in vitro; the associated mTORC1 mechanism was also investigated in zebrafish. Model: 18 newly reported individuals from 15 families, prior cases reviewed, in vitro assays and zebrafish modeling. Limitations: Likely mechanistic contribution, not proof that this pathway explains every patient feature. Evidence access: Primary abstract Clinical, neuroradiological, and molecular characterization of mitochondrial threonyl-tRNA-synthetase (TARS2)-related disorder. · 2023 · https://pubmed.ncbi.nlm.nih.gov/37454282/ · DOI 10.1016/j.gim.2023.100938
    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