Component

STAT3 palmitoylation in human cells

8 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 acts on it

  1. APT2-C2S expression did not reproduce the wild-type reduction in STAT3 palmitoylation.

    Human APT2 C2S expression in HEK293T → STAT3 palmitoylation in human cells source_derived_draftungraded
    Experimental context and source evidence
    experimental_model
    Human HEK293T with expressed APT2 and Flag-STAT3
    exposure
    Expression constructs; 50 micromolar Alk14 labeling for 5 hours; expression duration unresolved.
    limitations
    C2S disrupts the APT2 palmitoylation site; S122A alters its catalytic site. They are not interchangeable controls. Null results do not establish equivalence. GPX4 was not an endpoint.
    organism
    Human
    primary_locator
    Figure 2d; Extended Data 7b-c.
    primary_references
    https://doi.org/10.1038/s41586-020-2799-2

    APT2-STAT3 cycling and a competing sulforaphane target route · lines 51–57

    Selected primary observations: 10.1038/s41586-020-2799-2 and 10.1038/s41388-020-1335-z. · supports · Human HEK293T with expressed APT2 and Flag-STAT3 · source_derived_draft · unverified_draft

    APT2-C2S expression did not reproduce the wild-type reduction in STAT3 palmitoylation. primary_references: https://doi.org/10.1038/s41586-020-2799-2 primary_locator: Figure 2d; Extended Data 7b-c. organism: Human experimental_model: Human HEK293T with expressed APT2 and Flag-STAT3 exposure: Expression constructs; 50 micromolar Alk14 labeling for 5 hours; expression duration unresolved. limitations: C2S disrupts the APT2 palmitoylation site; S122A alters its catalytic site. They are not interchangeable controls. Null results do not establish equivalence. GPX4 was not an endpoint.
    Complete structured claim and evidence

  2. LYPLA2 siRNA increased STAT3 palmitoylation in the reported reconstituted HEK293T experiment.

    Human APT2/LYPLA2 knockdown in HEK293T → STAT3 palmitoylation in human cells source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    experimental_model
    Human HEK293T; DHHC7 knockout reconstituted with HA-DHHC7 and Flag-STAT3; DHHC construct species is not established as human for this figure.
    exposure
    LYPLA2 siRNA before Alk14 labeling; Figure 2f states 36 hours before labeling; exact siRNA amount unresolved.
    limitations
    Reported cellular result, not a GPX4 time-course experiment. Overexpressed DHHC constructs in much of the study are mouse proteins; human constructs are explicitly identified only where confirmed. APT2 depletion, selective inhibitor exposure and sulforaphane are different interventions.
    organism
    Human
    primary_locator
    Figure 2f; Extended Data 7d.
    primary_references
    https://doi.org/10.1038/s41586-020-2799-2
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    APT2-STAT3 cycling and a competing sulforaphane target route · lines 15–21

    Selected primary observations: 10.1038/s41586-020-2799-2 and 10.1038/s41388-020-1335-z. · supports · Human HEK293T; DHHC7 knockout reconstituted with HA-DHHC7 and Flag-STAT3; DHHC construct species is not established as human for this figure. · source_derived_draft · unverified_draft

    LYPLA2 siRNA increased STAT3 palmitoylation in the reported reconstituted HEK293T experiment. primary_references: https://doi.org/10.1038/s41586-020-2799-2 primary_locator: Figure 2f; Extended Data 7d. organism: Human experimental_model: Human HEK293T; DHHC7 knockout reconstituted with HA-DHHC7 and Flag-STAT3; DHHC construct species is not established as human for this figure. exposure: LYPLA2 siRNA before Alk14 labeling; Figure 2f states 36 hours before labeling; exact siRNA amount unresolved. limitations: Reported cellular result, not a GPX4 time-course experiment. Overexpressed DHHC constructs in much of the study are mouse proteins; human constructs are explicitly identified only where confirmed. APT2 depletion, selective inhibitor exposure and sulforaphane are different interventions.
    Complete structured claim and evidence

  3. APT2-S122A expression did not reproduce the wild-type reduction in STAT3 palmitoylation.

    Human APT2 S122A expression in HEK293T → STAT3 palmitoylation in human cells source_derived_draftungraded
    Experimental context and source evidence
    experimental_model
    Human HEK293T with expressed APT2 and Flag-STAT3
    exposure
    Expression constructs; 50 micromolar Alk14 labeling for 5 hours; expression duration unresolved.
    limitations
    C2S disrupts the APT2 palmitoylation site; S122A alters its catalytic site. They are not interchangeable controls. Null results do not establish equivalence. GPX4 was not an endpoint.
    organism
    Human
    primary_locator
    Figure 2d; Extended Data 7b-c.
    primary_references
    https://doi.org/10.1038/s41586-020-2799-2

    APT2-STAT3 cycling and a competing sulforaphane target route · lines 60–66

    Selected primary observations: 10.1038/s41586-020-2799-2 and 10.1038/s41388-020-1335-z. · supports · Human HEK293T with expressed APT2 and Flag-STAT3 · source_derived_draft · unverified_draft

    APT2-S122A expression did not reproduce the wild-type reduction in STAT3 palmitoylation. primary_references: https://doi.org/10.1038/s41586-020-2799-2 primary_locator: Figure 2d; Extended Data 7b-c. organism: Human experimental_model: Human HEK293T with expressed APT2 and Flag-STAT3 exposure: Expression constructs; 50 micromolar Alk14 labeling for 5 hours; expression duration unresolved. limitations: C2S disrupts the APT2 palmitoylation site; S122A alters its catalytic site. They are not interchangeable controls. Null results do not establish equivalence. GPX4 was not an endpoint.
    Complete structured claim and evidence

  4. Wild-type APT2 expression reduced STAT3 palmitoylation.

    Human APT2 WT expression in HEK293T → STAT3 palmitoylation in human cells source_derived_draftungraded
    Experimental context and source evidence
    experimental_model
    Human HEK293T with expressed APT2 and Flag-STAT3
    exposure
    Expression constructs; 50 micromolar Alk14 labeling for 5 hours; expression duration unresolved.
    limitations
    C2S disrupts the APT2 palmitoylation site; S122A alters its catalytic site. They are not interchangeable controls. Null results do not establish equivalence. GPX4 was not an endpoint.
    organism
    Human
    primary_locator
    Figure 2d; Extended Data 7b-c.
    primary_references
    https://doi.org/10.1038/s41586-020-2799-2

    APT2-STAT3 cycling and a competing sulforaphane target route · lines 42–48

    Selected primary observations: 10.1038/s41586-020-2799-2 and 10.1038/s41388-020-1335-z. · supports · Human HEK293T with expressed APT2 and Flag-STAT3 · source_derived_draft · unverified_draft

    Wild-type APT2 expression reduced STAT3 palmitoylation. primary_references: https://doi.org/10.1038/s41586-020-2799-2 primary_locator: Figure 2d; Extended Data 7b-c. organism: Human experimental_model: Human HEK293T with expressed APT2 and Flag-STAT3 exposure: Expression constructs; 50 micromolar Alk14 labeling for 5 hours; expression duration unresolved. limitations: C2S disrupts the APT2 palmitoylation site; S122A alters its catalytic site. They are not interchangeable controls. Null results do not establish equivalence. GPX4 was not an endpoint.
    Complete structured claim and evidence

  5. Human ZDHHC7 expression increased STAT3 palmitoylation in the human-construct confirmation experiment.

    Human ZDHHC7 expression in HEK293T → STAT3 palmitoylation in human cells source_derived_draftungraded
    Experimental context and source evidence
    experimental_model
    Human HEK293T expressing human DHHC proteins
    exposure
    Comparison of Flag-tagged human DHHC3, DHHC7 and DHHC19 with HA-STAT3; Alk14 assay.
    limitations
    Human-construct confirmation is separate from the mouse-DHHC screening experiments. Selected result/legend reviewed; raw gel intensities not reanalyzed.
    organism
    Human
    primary_locator
    Extended Data Figure 2f; Results: STAT3 is palmitoylated by DHHC7.
    primary_references
    https://doi.org/10.1038/s41586-020-2799-2

    APT2-STAT3 cycling and a competing sulforaphane target route · lines 69–75

    Selected primary observations: 10.1038/s41586-020-2799-2 and 10.1038/s41388-020-1335-z. · supports · Human HEK293T expressing human DHHC proteins · source_derived_draft · unverified_draft

    Human ZDHHC7 expression increased STAT3 palmitoylation in the human-construct confirmation experiment. primary_references: https://doi.org/10.1038/s41586-020-2799-2 primary_locator: Extended Data Figure 2f; Results: STAT3 is palmitoylated by DHHC7. organism: Human experimental_model: Human HEK293T expressing human DHHC proteins exposure: Comparison of Flag-tagged human DHHC3, DHHC7 and DHHC19 with HA-STAT3; Alk14 assay. limitations: Human-construct confirmation is separate from the mouse-DHHC screening experiments. Selected result/legend reviewed; raw gel intensities not reanalyzed.
    Complete structured claim and evidence

  6. ML349 increased STAT3 palmitoylation in the reported reconstituted HEK293T experiment.

    ML349, experimental APT2 inhibitor → STAT3 palmitoylation in human cells source_derived_draftungraded
    Experimental context and source evidence
    experimental_model
    Human HEK293T; DHHC7 knockout reconstituted with HA-DHHC7 and Flag-STAT3; DHHC construct species is not established as human for this figure.
    exposure
    20 micromolar ML349 for 36 hours before Alk14 labeling; labeling methods specify 50 micromolar Alk14 for 5 hours.
    limitations
    Reported cellular result, not a GPX4 time-course experiment. Overexpressed DHHC constructs in much of the study are mouse proteins; human constructs are explicitly identified only where confirmed. APT2 depletion, selective inhibitor exposure and sulforaphane are different interventions.
    organism
    Human
    primary_locator
    Figure 2f; Extended Data 7d; APT2 depalmitoylates p-STAT3.
    primary_references
    https://doi.org/10.1038/s41586-020-2799-2

    APT2-STAT3 cycling and a competing sulforaphane target route · lines 6–12

    Selected primary observations: 10.1038/s41586-020-2799-2 and 10.1038/s41388-020-1335-z. · supports · Human HEK293T; DHHC7 knockout reconstituted with HA-DHHC7 and Flag-STAT3; DHHC construct species is not established as human for this figure. · source_derived_draft · unverified_draft

    ML349 increased STAT3 palmitoylation in the reported reconstituted HEK293T experiment. primary_references: https://doi.org/10.1038/s41586-020-2799-2 primary_locator: Figure 2f; Extended Data 7d; APT2 depalmitoylates p-STAT3. organism: Human experimental_model: Human HEK293T; DHHC7 knockout reconstituted with HA-DHHC7 and Flag-STAT3; DHHC construct species is not established as human for this figure. exposure: 20 micromolar ML349 for 36 hours before Alk14 labeling; labeling methods specify 50 micromolar Alk14 for 5 hours. limitations: Reported cellular result, not a GPX4 time-course experiment. Overexpressed DHHC constructs in much of the study are mouse proteins; human constructs are explicitly identified only where confirmed. APT2 depletion, selective inhibitor exposure and sulforaphane are different interventions.
    Complete structured claim and evidence

  7. Solasonine did not increase STAT3 palmitoylation in the reported APT2-D13A/L11A mutant setting.

    APT2-D13A/L11A expression with solasonine in human gallbladder cancer cells → STAT3 palmitoylation in human cells source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    experimental_model
    Human NOZ and GBC-SD gallbladder cancer cells
    exposure
    Methods 2.2 describes 48-hour cellular drug treatments with refresh at 24 hours; exact concentration must be checked per figure and is not inferred from another assay.
    limitations
    Human cancer-cell experiments; no clinical or dietary inference. Solasonine exposure is not equivalent to APT2 depletion, ML349, or sulforaphane. Mutant rescue does not by itself establish selectivity or normal baseline mutant function. Figure 5C calls this APT2 activity, but Methods 2.17 describes an anti-LYPLA2 ELISA with mass-concentration standards and an HRP/TMB readout from cell supernatants. No direct APT2 substrate-turnover assay is described there. The result is retained as an author-labelled activity proxy, not established catalytic inhibition. This methodological qualification does not invalidate the separately reported binding or cellular observations.
    organism
    Human
    primary_locator
    Figure 6E; Supplementary Figure S5A; Results 3.6.
    primary_references
    https://doi.org/10.1002/ptr.70245
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    APT2, STAT3 and GPX4: opposing branches and assay qualification · lines 159–165

    Primary observations: 10.1038/s41467-025-56344-5 and 10.1002/ptr.70245; selected full-text review 2026-09-20. · supports · Human NOZ and GBC-SD gallbladder cancer cells · source_derived_draft · unverified_draft

    Solasonine did not increase STAT3 palmitoylation in the reported APT2-D13A/L11A mutant setting. primary_references: https://doi.org/10.1002/ptr.70245 primary_locator: Figure 6E; Supplementary Figure S5A; Results 3.6. organism: Human experimental_model: Human NOZ and GBC-SD gallbladder cancer cells exposure: Methods 2.2 describes 48-hour cellular drug treatments with refresh at 24 hours; exact concentration must be checked per figure and is not inferred from another assay. limitations: Human cancer-cell experiments; no clinical or dietary inference. Solasonine exposure is not equivalent to APT2 depletion, ML349, or sulforaphane. Mutant rescue does not by itself establish selectivity or normal baseline mutant function. Figure 5C calls this APT2 activity, but Methods 2.17 describes an anti-LYPLA2 ELISA with mass-concentration standards and an HRP/TMB readout from cell supernatants. No direct APT2 substrate-turnover assay is described there. The result is retained as an author-labelled activity proxy, not established catalytic inhibition. This methodological qualification does not invalidate the separately reported binding or cellular observations.
    Complete structured claim and evidence

  8. Solasonine increased STAT3 acyl-biotin-exchange signal.

    Solasonine → STAT3 palmitoylation in human cells source_derived_draftungraded
    Experimental context and source evidence
    experimental_model
    Human NOZ and GBC-SD gallbladder cancer cells
    exposure
    Methods 2.2 describes 48-hour cellular drug treatments with refresh at 24 hours; exact concentration must be checked per figure and is not inferred from another assay.
    limitations
    Human cancer-cell experiments; no clinical or dietary inference. Solasonine exposure is not equivalent to APT2 depletion, ML349, or sulforaphane. Mutant rescue does not by itself establish selectivity or normal baseline mutant function. Figure 5C calls this APT2 activity, but Methods 2.17 describes an anti-LYPLA2 ELISA with mass-concentration standards and an HRP/TMB readout from cell supernatants. No direct APT2 substrate-turnover assay is described there. The result is retained as an author-labelled activity proxy, not established catalytic inhibition. This methodological qualification does not invalidate the separately reported binding or cellular observations.
    organism
    Human
    primary_locator
    Figure 5A; Supplementary Figure S4A; Results 3.5.
    primary_references
    https://doi.org/10.1002/ptr.70245

    APT2, STAT3 and GPX4: opposing branches and assay qualification · lines 69–75

    Primary observations: 10.1038/s41467-025-56344-5 and 10.1002/ptr.70245; selected full-text review 2026-09-20. · supports · Human NOZ and GBC-SD gallbladder cancer cells · source_derived_draft · unverified_draft

    Solasonine increased STAT3 acyl-biotin-exchange signal. primary_references: https://doi.org/10.1002/ptr.70245 primary_locator: Figure 5A; Supplementary Figure S4A; Results 3.5. organism: Human experimental_model: Human NOZ and GBC-SD gallbladder cancer cells exposure: Methods 2.2 describes 48-hour cellular drug treatments with refresh at 24 hours; exact concentration must be checked per figure and is not inferred from another assay. limitations: Human cancer-cell experiments; no clinical or dietary inference. Solasonine exposure is not equivalent to APT2 depletion, ML349, or sulforaphane. Mutant rescue does not by itself establish selectivity or normal baseline mutant function. Figure 5C calls this APT2 activity, but Methods 2.17 describes an anti-LYPLA2 ELISA with mass-concentration standards and an HRP/TMB readout from cell supernatants. No direct APT2 substrate-turnover assay is described there. The result is retained as an author-labelled activity proxy, not established catalytic inhibition. This methodological qualification does not invalidate the separately reported binding or cellular observations.
    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