Component

Mouse acyl-protein thioesterase 2 / LYPLA2

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

Where it participates (unsigned role)

  1. IFNAR deficiency reduced infected-red-cell-induced APT2 transcript expression in peritoneal macrophages.

    Mouse IFNAR-deficient peritoneal macrophages → APT2 transcript abundance in mouse cells source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    experimental_model
    Mouse wild-type versus Ifnar-deficient peritoneal exudate macrophages
    exposure
    Freeze-thawed Plasmodium yoelii N67 infected red blood cells at 0, 6, 12 and 24 hours (Figure 7d visually reviewed).
    limitations
    The manuscript calls the genotype Ifnar-deficient; this extraction does not assign a specific disrupted subunit allele. No specific IFNAR1 or IFNAR2 state link is inferred.
    organism
    Mouse
    primary_locator
    Figure 7d; RT-qPCR and Results.
    primary_references
    https://doi.org/10.1038/s41467-025-65081-8
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    MAVS inhibitor nulls and APT2-TBK1 immune feedback · lines 96–102

    Selected primary observations: 10.1073/pnas.2403392121; 10.1038/s41467-025-65081-8. · supports · Mouse wild-type versus Ifnar-deficient peritoneal exudate macrophages · source_derived_draft · unverified_draft

    IFNAR deficiency reduced infected-red-cell-induced APT2 transcript expression in peritoneal macrophages. primary_references: https://doi.org/10.1038/s41467-025-65081-8 primary_locator: Figure 7d; RT-qPCR and Results. organism: Mouse experimental_model: Mouse wild-type versus Ifnar-deficient peritoneal exudate macrophages exposure: Freeze-thawed Plasmodium yoelii N67 infected red blood cells at 0, 6, 12 and 24 hours (Figure 7d visually reviewed). limitations: The manuscript calls the genotype Ifnar-deficient; this extraction does not assign a specific disrupted subunit allele. No specific IFNAR1 or IFNAR2 state link is inferred.
    Complete structured claim and evidence

  2. Recombinant mouse IFN-beta increased APT2 protein expression in peritoneal macrophages.

    Mouse interferon beta / IFNB1 → APT2 protein abundance in mouse cells source_derived_draftungraded
    Experimental context and source evidence
    experimental_model
    Mouse peritoneal exudate macrophages
    exposure
    Recombinant IFN-beta at 0, 3, 6 and 12 hours (Figure 7c visually reviewed); exact dose unresolved.
    limitations
    No measurement of APT2 membrane localization, catalytic flux or GPX4 turnover. Protein induction does not establish increased activity toward every APT2 substrate.
    organism
    Mouse
    primary_locator
    Figure 7c; immunoblot and corresponding Results.
    primary_references
    https://doi.org/10.1038/s41467-025-65081-8

    MAVS inhibitor nulls and APT2-TBK1 immune feedback · lines 87–93

    Selected primary observations: 10.1073/pnas.2403392121; 10.1038/s41467-025-65081-8. · supports · Mouse peritoneal exudate macrophages · source_derived_draft · unverified_draft

    Recombinant mouse IFN-beta increased APT2 protein expression in peritoneal macrophages. primary_references: https://doi.org/10.1038/s41467-025-65081-8 primary_locator: Figure 7c; immunoblot and corresponding Results. organism: Mouse experimental_model: Mouse peritoneal exudate macrophages exposure: Recombinant IFN-beta at 0, 3, 6 and 12 hours (Figure 7c visually reviewed); exact dose unresolved. limitations: No measurement of APT2 membrane localization, catalytic flux or GPX4 turnover. Protein induction does not establish increased activity toward every APT2 substrate.
    Complete structured claim and evidence

  3. LYPLA2 knockout prevented the reported stimulus-associated decline in TBK1 palmitoylation.

    Mouse LYPLA2 knockout in RAW 264.7 → TBK1 palmitoylation in mouse cells source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    experimental_model
    Mouse RAW 264.7; wild-type versus Lypla2 knockout
    exposure
    Plasmodium gDNA stimulation for 12 hours; concentration unresolved in this extraction.
    limitations
    Positive denotes preservation relative to stimulated wild-type, not an unqualified increase above resting baseline. No GPX4 endpoint.
    organism
    Mouse
    primary_locator
    Figure 3c; ABE and immunoblot.
    primary_references
    https://doi.org/10.1038/s41467-025-65081-8
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    MAVS inhibitor nulls and APT2-TBK1 immune feedback · lines 78–84

    Selected primary observations: 10.1073/pnas.2403392121; 10.1038/s41467-025-65081-8. · supports · Mouse RAW 264.7; wild-type versus Lypla2 knockout · source_derived_draft · unverified_draft

    LYPLA2 knockout prevented the reported stimulus-associated decline in TBK1 palmitoylation. primary_references: https://doi.org/10.1038/s41467-025-65081-8 primary_locator: Figure 3c; ABE and immunoblot. organism: Mouse experimental_model: Mouse RAW 264.7; wild-type versus Lypla2 knockout exposure: Plasmodium gDNA stimulation for 12 hours; concentration unresolved in this extraction. limitations: Positive denotes preservation relative to stimulated wild-type, not an unqualified increase above resting baseline. No GPX4 endpoint.
    Complete structured claim and evidence

  4. ML349 increased the reported IRF3 phosphorylation response despite MAVS knockout in stimulated RAW 264.7 cells.

    ML349, experimental APT2 inhibitor → IRF3 phosphorylation in mouse cells source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    experimental_model
    Mouse RAW 264.7; Mavs knockout
    exposure
    ML349 10 micromolar for 12 hours, then freeze-thawed Plasmodium yoelii N67 infected red blood cells for 6 hours.
    limitations
    MAVS loss reduces the baseline response. TBK1 loss removes a central signaling node; failure of rescue supports dependence but does not alone prove direct ML349 binding to TBK1. Not a viral infection experiment.
    organism
    Mouse
    primary_locator
    Figure 4j and corresponding Results; IFN-I activation is assessed here by immunoblot, not secreted interferon measurement.
    primary_references
    https://doi.org/10.1038/s41467-025-65081-8
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    MAVS inhibitor nulls and APT2-TBK1 immune feedback · lines 51–57

    Selected primary observations: 10.1073/pnas.2403392121; 10.1038/s41467-025-65081-8. · supports · Mouse RAW 264.7; Mavs knockout · source_derived_draft · unverified_draft

    ML349 increased the reported IRF3 phosphorylation response despite MAVS knockout in stimulated RAW 264.7 cells. primary_references: https://doi.org/10.1038/s41467-025-65081-8 primary_locator: Figure 4j and corresponding Results; IFN-I activation is assessed here by immunoblot, not secreted interferon measurement. organism: Mouse experimental_model: Mouse RAW 264.7; Mavs knockout exposure: ML349 10 micromolar for 12 hours, then freeze-thawed Plasmodium yoelii N67 infected red blood cells for 6 hours. limitations: MAVS loss reduces the baseline response. TBK1 loss removes a central signaling node; failure of rescue supports dependence but does not alone prove direct ML349 binding to TBK1. Not a viral infection experiment.
    Complete structured claim and evidence

  5. ML349 failed to restore the reported IRF3 phosphorylation response in TBK1-knockout RAW 264.7 cells.

    ML349, experimental APT2 inhibitor → IRF3 phosphorylation in mouse cells source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    experimental_model
    Mouse RAW 264.7; Tbk1 knockout
    exposure
    ML349 10 micromolar for 12 hours, then freeze-thawed Plasmodium yoelii N67 infected red blood cells for 6 hours.
    limitations
    MAVS loss reduces the baseline response. TBK1 loss removes a central signaling node; failure of rescue supports dependence but does not alone prove direct ML349 binding to TBK1. Not a viral infection experiment.
    organism
    Mouse
    primary_locator
    Figure 4j and corresponding Results; IFN-I activation is assessed here by immunoblot, not secreted interferon measurement.
    primary_references
    https://doi.org/10.1038/s41467-025-65081-8
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    MAVS inhibitor nulls and APT2-TBK1 immune feedback · lines 60–66

    Selected primary observations: 10.1073/pnas.2403392121; 10.1038/s41467-025-65081-8. · supports · Mouse RAW 264.7; Tbk1 knockout · source_derived_draft · unverified_draft

    ML349 failed to restore the reported IRF3 phosphorylation response in TBK1-knockout RAW 264.7 cells. primary_references: https://doi.org/10.1038/s41467-025-65081-8 primary_locator: Figure 4j and corresponding Results; IFN-I activation is assessed here by immunoblot, not secreted interferon measurement. organism: Mouse experimental_model: Mouse RAW 264.7; Tbk1 knockout exposure: ML349 10 micromolar for 12 hours, then freeze-thawed Plasmodium yoelii N67 infected red blood cells for 6 hours. limitations: MAVS loss reduces the baseline response. TBK1 loss removes a central signaling node; failure of rescue supports dependence but does not alone prove direct ML349 binding to TBK1. Not a viral infection experiment.
    Complete structured claim and evidence

  6. ML349 increased TBK1 palmitoylation in mouse peritoneal macrophages.

    ML349, experimental APT2 inhibitor → TBK1 palmitoylation in mouse cells source_derived_draftungraded
    Experimental context and source evidence
    experimental_model
    Mouse peritoneal exudate macrophages
    exposure
    ML349 concentration series for 12 hours; individual concentrations not transcribed from figure.
    limitations
    Concentration-response result; ABE is an S-acylation assay. No GPX4 endpoint in this experiment.
    organism
    Mouse
    primary_locator
    Figure 3b; ABE and immunoblot.
    primary_references
    https://doi.org/10.1038/s41467-025-65081-8

    MAVS inhibitor nulls and APT2-TBK1 immune feedback · lines 69–75

    Selected primary observations: 10.1073/pnas.2403392121; 10.1038/s41467-025-65081-8. · supports · Mouse peritoneal exudate macrophages · source_derived_draft · unverified_draft

    ML349 increased TBK1 palmitoylation in mouse peritoneal macrophages. primary_references: https://doi.org/10.1038/s41467-025-65081-8 primary_locator: Figure 3b; ABE and immunoblot. organism: Mouse experimental_model: Mouse peritoneal exudate macrophages exposure: ML349 concentration series for 12 hours; individual concentrations not transcribed from figure. limitations: Concentration-response result; ABE is an S-acylation assay. No GPX4 endpoint in this experiment.
    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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