Component

Mouse eIF5A translation factor

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

5 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. Hypusination disruption lowered expression of methylmalonyl-CoA mutase; its mitochondrial targeting sequence increased reporter dependence on eIF5A.

    Mouse eIF5A translation factor → Mouse methylmalonyl-CoA mutase / MMUT source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary full text
    experimental_model
    Mouse macrophage/MEF protein experiments and targeting-sequence reporters.
    limitations
    This is protein expression, not proof of riboflavin, CoA or B12 deficiency; the relevant cofactor requires separate evidence.
    nutrient_topic
    Spermidine collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Spermidine
    plain_language
    Making a cofactor-dependent enzyme is another potential bottleneck.
    primary_references
    Polyamines and eIF5A Hypusination Modulate Mitochondrial Respiration and Macrophage Activation. · 2019 · https://pubmed.ncbi.nlm.nih.gov/31130465/ · DOI 10.1016/j.cmet.2019.05.003

    Spermidine: biosynthesis, hypusination, transport 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 · Mouse macrophage/MEF protein experiments and targeting-sequence reporters. · source_derived_draft · unverified_draft

    ## spermidine-mitochondrial-target-mmut Making a cofactor-dependent enzyme is another potential bottleneck. Hypusination disruption lowered expression of methylmalonyl-CoA mutase; its mitochondrial targeting sequence increased reporter dependence on eIF5A. Model: Mouse macrophage/MEF protein experiments and targeting-sequence reporters. Limitations: This is protein expression, not proof of riboflavin, CoA or B12 deficiency; the relevant cofactor requires separate evidence. Evidence access: Primary full text Polyamines and eIF5A Hypusination Modulate Mitochondrial Respiration and Macrophage Activation. · 2019 · https://pubmed.ncbi.nlm.nih.gov/31130465/ · DOI 10.1016/j.cmet.2019.05.003
    Complete structured claim and evidence

  2. Hypusination disruption lowered expression of succinate dehydrogenase subunit A; its mitochondrial targeting sequence increased reporter dependence on eIF5A.

    Mouse eIF5A translation factor → Mouse succinate dehydrogenase subunit A / SDHA source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary full text
    experimental_model
    Mouse macrophage/MEF protein experiments and targeting-sequence reporters.
    limitations
    This is protein expression, not proof of riboflavin, CoA or B12 deficiency; the relevant cofactor requires separate evidence.
    nutrient_topic
    Spermidine collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Spermidine
    plain_language
    Making a cofactor-dependent enzyme is another potential bottleneck.
    primary_references
    Polyamines and eIF5A Hypusination Modulate Mitochondrial Respiration and Macrophage Activation. · 2019 · https://pubmed.ncbi.nlm.nih.gov/31130465/ · DOI 10.1016/j.cmet.2019.05.003

    Spermidine: biosynthesis, hypusination, transport and cross-nutrient mechanisms (2026-09-19) · lines 270–276

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Mouse macrophage/MEF protein experiments and targeting-sequence reporters. · source_derived_draft · unverified_draft

    ## spermidine-mitochondrial-target-sdha Making a cofactor-dependent enzyme is another potential bottleneck. Hypusination disruption lowered expression of succinate dehydrogenase subunit A; its mitochondrial targeting sequence increased reporter dependence on eIF5A. Model: Mouse macrophage/MEF protein experiments and targeting-sequence reporters. Limitations: This is protein expression, not proof of riboflavin, CoA or B12 deficiency; the relevant cofactor requires separate evidence. Evidence access: Primary full text Polyamines and eIF5A Hypusination Modulate Mitochondrial Respiration and Macrophage Activation. · 2019 · https://pubmed.ncbi.nlm.nih.gov/31130465/ · DOI 10.1016/j.cmet.2019.05.003
    Complete structured claim and evidence

  3. Hypusination disruption lowered expression of succinyl-CoA ligase alpha; its mitochondrial targeting sequence increased reporter dependence on eIF5A.

    Mouse eIF5A translation factor → Mouse succinyl-CoA ligase alpha / SUCLG1 source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary full text
    experimental_model
    Mouse macrophage/MEF protein experiments and targeting-sequence reporters.
    limitations
    This is protein expression, not proof of riboflavin, CoA or B12 deficiency; the relevant cofactor requires separate evidence.
    nutrient_topic
    Spermidine collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Spermidine
    plain_language
    Making a cofactor-dependent enzyme is another potential bottleneck.
    primary_references
    Polyamines and eIF5A Hypusination Modulate Mitochondrial Respiration and Macrophage Activation. · 2019 · https://pubmed.ncbi.nlm.nih.gov/31130465/ · DOI 10.1016/j.cmet.2019.05.003

    Spermidine: biosynthesis, hypusination, transport and cross-nutrient mechanisms (2026-09-19) · lines 278–284

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Mouse macrophage/MEF protein experiments and targeting-sequence reporters. · source_derived_draft · unverified_draft

    ## spermidine-mitochondrial-target-suclg1 Making a cofactor-dependent enzyme is another potential bottleneck. Hypusination disruption lowered expression of succinyl-CoA ligase alpha; its mitochondrial targeting sequence increased reporter dependence on eIF5A. Model: Mouse macrophage/MEF protein experiments and targeting-sequence reporters. Limitations: This is protein expression, not proof of riboflavin, CoA or B12 deficiency; the relevant cofactor requires separate evidence. Evidence access: Primary full text Polyamines and eIF5A Hypusination Modulate Mitochondrial Respiration and Macrophage Activation. · 2019 · https://pubmed.ncbi.nlm.nih.gov/31130465/ · DOI 10.1016/j.cmet.2019.05.003
    Complete structured claim and evidence

  4. Satellite-cell eIF5A knockout reduced MyoD translation and impaired the spermidine-associated activation response.

    Mouse eIF5A translation factor → Mouse myogenic differentiation 1 / Myod1 source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    evidence_access
    Primary full text
    experimental_model
    Mouse satellite-cell knockout, ribosome profiling and translation experiments.
    limitations
    Dependency does not show that every muscle protein is similarly regulated.
    nutrient_topic
    Spermidine collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Spermidine
    plain_language
    A specific muscle-regulating protein is a translation target.
    primary_references
    Spermidine-eIF5A axis is essential for muscle stem cell activation via translational control. · 2024 · https://pubmed.ncbi.nlm.nih.gov/39251577/ · DOI 10.1038/s41421-024-00712-w
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    Spermidine: biosynthesis, hypusination, transport and cross-nutrient mechanisms (2026-09-19) · lines 382–388

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Mouse satellite-cell knockout, ribosome profiling and translation experiments. · source_derived_draft · unverified_draft

    ## spermidine-myod-translation A specific muscle-regulating protein is a translation target. Satellite-cell eIF5A knockout reduced MyoD translation and impaired the spermidine-associated activation response. Model: Mouse satellite-cell knockout, ribosome profiling and translation experiments. Limitations: Dependency does not show that every muscle protein is similarly regulated. Evidence access: Primary full text Spermidine-eIF5A axis is essential for muscle stem cell activation via translational control. · 2024 · https://pubmed.ncbi.nlm.nih.gov/39251577/ · DOI 10.1038/s41421-024-00712-w
    Complete structured claim and evidence

  5. Disrupting eIF5A hypusination reduced nascent TFEB synthesis in the B-cell/autophagy study.

    Mouse eIF5A translation factor → Mouse transcription factor EB / Tfeb source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary full text
    experimental_model
    Mouse cellular experiments with translation labeling and hypusination perturbation.
    limitations
    Requirement is transcript- and context-dependent, not equal enhancement of all proteins.
    nutrient_topic
    Spermidine collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Spermidine
    plain_language
    Spermidine helps produce a regulator of cellular recycling.
    primary_references
    Polyamines Control eIF5A Hypusination, TFEB Translation, and Autophagy to Reverse B Cell Senescence. · 2019 · https://pubmed.ncbi.nlm.nih.gov/31474573/ · DOI 10.1016/j.molcel.2019.08.005

    Spermidine: biosynthesis, hypusination, transport and cross-nutrient mechanisms (2026-09-19) · lines 214–220

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Mouse cellular experiments with translation labeling and hypusination perturbation. · source_derived_draft · unverified_draft

    ## spermidine-tfeb-translation Spermidine helps produce a regulator of cellular recycling. Disrupting eIF5A hypusination reduced nascent TFEB synthesis in the B-cell/autophagy study. Model: Mouse cellular experiments with translation labeling and hypusination perturbation. Limitations: Requirement is transcript- and context-dependent, not equal enhancement of all proteins. Evidence access: Primary full text Polyamines Control eIF5A Hypusination, TFEB Translation, and Autophagy to Reverse B Cell Senescence. · 2019 · https://pubmed.ncbi.nlm.nih.gov/31474573/ · DOI 10.1016/j.molcel.2019.08.005
    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