Component

RAC1

Independent biological entity. Read linked claims for experimental scope and context.

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. Loss of Rac1 activity strongly inhibited respiratory syncytial virus through a decrease in F protein surface expression.

    RAC1 → Respiratory syncytial virus F protein surface expression source_derived_draftungraded
    Experimental context and source evidence
    duration
    Not stated here
    evidence_access
    Primary PubMed abstract and indexed metadata reviewed. Full-text method details not stated here remain unresolved.
    experimental_model
    Human cell culture
    exposure
    Rac1 activity loss under statin or geranylgeranyltransferase inhibition
    limitations
    Rac1 was the strongest of the Rho-family GTPases assayed in that study; the others were not equivalent.
    organism
    Human cell culture
    plain_language
    Loss of Rac1 activity strongly inhibited respiratory syncytial virus through a decrease in F protein surface expression.
    primary_references
    Statin-mediated disruption of Rho GTPase prenylation and activity inhibits respiratory syncytial virus infection. (2021). https://pubmed.ncbi.nlm.nih.gov/34716403/ DOI: 10.1038/s42003-021-02754-2
    route
    In vitro
    tissue
    Rho-family GTPase activity and viral fusion protein surface expression

    Atorvastatin: mechanism of action from target occupancy to isoprenoids, transport, muscle and metabolism (2026-09-22) · lines 100–109

    Original AI-assisted curation of twelve primary studies resolved by PubMed title search and cross-checked against live PubMed metadata. Findings obtained with mevastatin, simvastatin or the statin class are recorded against those subjects. Study-specific citations, doses, negative findings and limitations retained. Not publisher full text. · supports · · source_derived_draft · unverified_draft

    ## rac1-supports-viral-f-protein-surface-expression Loss of Rac1 activity strongly inhibited respiratory syncytial virus through a decrease in F protein surface expression. Model/species: Human cell culture Tissue/system: Rho-family GTPase activity and viral fusion protein surface expression Exposure: Rac1 activity loss under statin or geranylgeranyltransferase inhibition Route: In vitro Duration: Not stated here Limits: Rac1 was the strongest of the Rho-family GTPases assayed in that study; the others were not equivalent. Primary reference: Statin-mediated disruption of Rho GTPase prenylation and activity inhibits respiratory syncytial virus infection. (2021). https://pubmed.ncbi.nlm.nih.gov/34716403/ DOI: 10.1038/s42003-021-02754-2 Access: Primary PubMed abstract and indexed metadata reviewed. Full-text method details not stated here remain unresolved.
    Complete structured claim and evidence

What acts on it

  1. Silencing STAT3 or JAK2 did not reproduce cucurbitacin I-mediated Rac1 inhibition in the tested human breast-cancer cells.

    STAT3 → RAC1 source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    evidence_access
    Primary abstract
    experimental_model
    RNA interference in human breast-cancer cells.
    limitations
    Negative pathway test is limited to these endpoints and cells; it does not show that all JAK/STAT effects are absent.
    nutrient_topic
    Cucurbitacins collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Cucurbitacins
    plain_language
    Removing the familiar signaling pathway did not explain this movement effect.
    primary_references
    Cucurbitacin I inhibits Rac1 activation in breast cancer cells by a reactive oxygen species-mediated mechanism and independently of Janus tyrosine kinase 2 and P-Rex1. · 2013 · https://pubmed.ncbi.nlm.nih.gov/23478800/ · DOI 10.1124/mol.112.084293
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    Cucurbitacins: thiol chemistry, cytoskeleton, metabolic dependencies and signaling (2026-09-20) · lines 172–178

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · RNA interference in human breast-cancer cells. · source_derived_draft · unverified_draft

    ## cucurbitacin-i-jak-stat-knockdown Removing the familiar signaling pathway did not explain this movement effect. Silencing STAT3 or JAK2 did not reproduce cucurbitacin I-mediated Rac1 inhibition in the tested human breast-cancer cells. Model: RNA interference in human breast-cancer cells. Limitations: Negative pathway test is limited to these endpoints and cells; it does not show that all JAK/STAT effects are absent. Evidence access: Primary abstract Cucurbitacin I inhibits Rac1 activation in breast cancer cells by a reactive oxygen species-mediated mechanism and independently of Janus tyrosine kinase 2 and P-Rex1. · 2013 · https://pubmed.ncbi.nlm.nih.gov/23478800/ · DOI 10.1124/mol.112.084293
    Complete structured claim and evidence

  2. Mito-TEMPO and NAC prevented tested cucurbitacin I effects on Rac1 activation, supporting mitochondrial ROS involvement alongside the thiol-interception caveat for NAC.

    Mito-TEMPO → RAC1 source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Human breast-cancer pharmacology.
    limitations
    Probe rescue does not identify the ROS-generating enzyme or prove the same route after human ingestion.
    nutrient_topic
    Cucurbitacins collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Cucurbitacins
    plain_language
    Two different probes help test the oxidative-stress route.
    primary_references
    Cucurbitacin I inhibits Rac1 activation in breast cancer cells by a reactive oxygen species-mediated mechanism and independently of Janus tyrosine kinase 2 and P-Rex1. · 2013 · https://pubmed.ncbi.nlm.nih.gov/23478800/ · DOI 10.1124/mol.112.084293

    Cucurbitacins: thiol chemistry, cytoskeleton, metabolic dependencies and signaling (2026-09-20) · lines 180–186

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human breast-cancer pharmacology. · source_derived_draft · unverified_draft

    ## cucurbitacin-i-mitoros-rescue Two different probes help test the oxidative-stress route. Mito-TEMPO and NAC prevented tested cucurbitacin I effects on Rac1 activation, supporting mitochondrial ROS involvement alongside the thiol-interception caveat for NAC. Model: Human breast-cancer pharmacology. Limitations: Probe rescue does not identify the ROS-generating enzyme or prove the same route after human ingestion. Evidence access: Primary abstract Cucurbitacin I inhibits Rac1 activation in breast cancer cells by a reactive oxygen species-mediated mechanism and independently of Janus tyrosine kinase 2 and P-Rex1. · 2013 · https://pubmed.ncbi.nlm.nih.gov/23478800/ · DOI 10.1124/mol.112.084293
    Complete structured claim and evidence

  3. Cucurbitacin I reduced heregulin-evoked Rac1 activation in human breast-cancer cells.

    Cucurbitacin I → RAC1 source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Human breast-cancer cell experiments; representative 0.1 micromolar exposure for 1 hour.
    limitations
    Activity change is not direct Rac1 binding.
    nutrient_topic
    Cucurbitacins collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Cucurbitacins
    plain_language
    A movement-control switch became less active.
    primary_references
    Cucurbitacin I inhibits Rac1 activation in breast cancer cells by a reactive oxygen species-mediated mechanism and independently of Janus tyrosine kinase 2 and P-Rex1. · 2013 · https://pubmed.ncbi.nlm.nih.gov/23478800/ · DOI 10.1124/mol.112.084293

    Cucurbitacins: thiol chemistry, cytoskeleton, metabolic dependencies and signaling (2026-09-20) · lines 156–162

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human breast-cancer cell experiments; representative 0.1 micromolar exposure for 1 hour. · source_derived_draft · unverified_draft

    ## cucurbitacin-i-rac1 A movement-control switch became less active. Cucurbitacin I reduced heregulin-evoked Rac1 activation in human breast-cancer cells. Model: Human breast-cancer cell experiments; representative 0.1 micromolar exposure for 1 hour. Limitations: Activity change is not direct Rac1 binding. Evidence access: Primary abstract Cucurbitacin I inhibits Rac1 activation in breast cancer cells by a reactive oxygen species-mediated mechanism and independently of Janus tyrosine kinase 2 and P-Rex1. · 2013 · https://pubmed.ncbi.nlm.nih.gov/23478800/ · DOI 10.1124/mol.112.084293
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. Insulin increased TRPM6 surface abundance and channel activity through a PI3K- and RAC1-dependent pathway.

    Insulin → TRPM6 abundance at the cell surface source_derived_draftungraded
    Experimental context and source evidence
    cross_nutrient
    Insulin -> magnesium-channel trafficking; complements the separate Mg -> insulin-response findings.
    experimental_model
    Expression-cell electrophysiology and surface fluorescence.
    limitations
    Combined pathway perturbations; no unspecified PI3K isoform assigned and no universal clinical feedback loop proven.
    nutrient_topic
    Magnesium research collection; topical membership is not evidence of a direct dietary effect. · Magnesium
    organism
    Homo sapiens
    plain_language
    Insulin can affect the magnesium entry machinery as well as glucose metabolism.
    primary_references
    [mg-nair2012] Loss of insulin-induced activation of TRPM6 magnesium channels results in impaired glucose tolerance during pregnancy (2012). https://pubmed.ncbi.nlm.nih.gov/22733750/ DOI: 10.1073/pnas.1113811109
    tissue_or_cell_type
    TRPM6-expressing cells; plasma membrane

    Magnesium: cross-nutrient mechanisms and deficiency (2026-09-17) · lines 1527–1537

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Expression-cell electrophysiology and surface fluorescence. · source_derived_draft · unverified_draft

    ### mg-insulin-trpm6-surface-regulation Insulin increased TRPM6 surface abundance and channel activity through a PI3K- and RAC1-dependent pathway. Condition category: normal nutrient_topic: Magnesium research collection; topical membership is not evidence of a direct dietary effect. plain_language: Insulin can affect the magnesium entry machinery as well as glucose metabolism. organism: Homo sapiens tissue_or_cell_type: TRPM6-expressing cells; plasma membrane experimental_model: Expression-cell electrophysiology and surface fluorescence. limitations: Combined pathway perturbations; no unspecified PI3K isoform assigned and no universal clinical feedback loop proven. cross_nutrient: Insulin -> magnesium-channel trafficking; complements the separate Mg -> insulin-response findings. [mg-nair2012] Loss of insulin-induced activation of TRPM6 magnesium channels results in impaired glucose tolerance during pregnancy (2012). https://pubmed.ncbi.nlm.nih.gov/22733750/ DOI: 10.1073/pnas.1113811109
    Complete structured claim and evidence

  2. Statin treatment reduced host protein prenylation including prenylation of Rho GTPases, and reduced respiratory syncytial virus infection in vitro through combined cholesterol and isoprenoid effects.

    Statin therapy as a drug class → Prenylation of Rho-family GTPases source_derived_draftungraded
    Experimental context and source evidence
    duration
    Not stated here
    evidence_access
    Primary PubMed abstract and indexed metadata reviewed. Full-text method details not stated here remain unresolved.
    experimental_model
    Live-cell high-content screen in human cell culture
    exposure
    Statins, and separately perillyl alcohol as a geranylgeranyltransferase inhibitor
    limitations
    The screen tested statins as a class without attributing the result to atorvastatin, and respiratory syncytial virus infection itself globally upregulated prenylation, so the baseline was not a resting cell.
    organism
    Live-cell high-content screen in human cell culture
    plain_language
    Statin treatment reduced host protein prenylation including prenylation of Rho GTPases, and reduced respiratory syncytial virus infection in vitro through combined cholesterol and isoprenoid effects.
    primary_references
    Statin-mediated disruption of Rho GTPase prenylation and activity inhibits respiratory syncytial virus infection. (2021). https://pubmed.ncbi.nlm.nih.gov/34716403/ DOI: 10.1038/s42003-021-02754-2
    route
    In vitro
    tissue
    Host protein prenylation and virus production

    Atorvastatin: mechanism of action from target occupancy to isoprenoids, transport, muscle and metabolism (2026-09-22) · lines 89–98

    Original AI-assisted curation of twelve primary studies resolved by PubMed title search and cross-checked against live PubMed metadata. Findings obtained with mevastatin, simvastatin or the statin class are recorded against those subjects. Study-specific citations, doses, negative findings and limitations retained. Not publisher full text. · supports · · source_derived_draft · unverified_draft

    ## statin-reduces-rho-gtpase-prenylation Statin treatment reduced host protein prenylation including prenylation of Rho GTPases, and reduced respiratory syncytial virus infection in vitro through combined cholesterol and isoprenoid effects. Model/species: Live-cell high-content screen in human cell culture Tissue/system: Host protein prenylation and virus production Exposure: Statins, and separately perillyl alcohol as a geranylgeranyltransferase inhibitor Route: In vitro Duration: Not stated here Limits: The screen tested statins as a class without attributing the result to atorvastatin, and respiratory syncytial virus infection itself globally upregulated prenylation, so the baseline was not a resting cell. Primary reference: Statin-mediated disruption of Rho GTPase prenylation and activity inhibits respiratory syncytial virus infection. (2021). https://pubmed.ncbi.nlm.nih.gov/34716403/ DOI: 10.1038/s42003-021-02754-2 Access: Primary PubMed abstract and indexed metadata reviewed. Full-text method details not stated here remain unresolved.
    Complete structured claim and evidence

  3. Cucurbitacin I activated RhoA/ROCK signaling; disrupting this pathway prevented the observed Rac1 inhibition.

    Cucurbitacin I → Human RhoA / RHOA source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Human breast-cancer cellular perturbation experiments.
    limitations
    ROCK isoform is not resolved in this record; pathway dependence does not establish a direct cucurbitacin target.
    nutrient_topic
    Cucurbitacins collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Cucurbitacins
    plain_language
    One cytoskeletal pathway helped suppress another.
    primary_references
    Cucurbitacin I inhibits Rac1 activation in breast cancer cells by a reactive oxygen species-mediated mechanism and independently of Janus tyrosine kinase 2 and P-Rex1. · 2013 · https://pubmed.ncbi.nlm.nih.gov/23478800/ · DOI 10.1124/mol.112.084293

    Cucurbitacins: thiol chemistry, cytoskeleton, metabolic dependencies and signaling (2026-09-20) · lines 164–170

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

    ## cucurbitacin-i-rhoa-rock One cytoskeletal pathway helped suppress another. Cucurbitacin I activated RhoA/ROCK signaling; disrupting this pathway prevented the observed Rac1 inhibition. Model: Human breast-cancer cellular perturbation experiments. Limitations: ROCK isoform is not resolved in this record; pathway dependence does not establish a direct cucurbitacin target. Evidence access: Primary abstract Cucurbitacin I inhibits Rac1 activation in breast cancer cells by a reactive oxygen species-mediated mechanism and independently of Janus tyrosine kinase 2 and P-Rex1. · 2013 · https://pubmed.ncbi.nlm.nih.gov/23478800/ · DOI 10.1124/mol.112.084293
    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