Component

Human zinc transporter 6 / ZnT6

Human SLC30A6 protein, partner of ZnT5 in the secretory pathway.

4 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. Extracellular zinc supplementation did not restore reduced TNAP activity in DT40 cells deficient in both ZnT5-ZnT6 and ZnT7 complexes.

    Zinc(II) ion → Tissue-nonspecific alkaline phosphatase ALPL / TNAP source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    cross_nutrient
    false
    experimental_model
    Engineered chicken DT40 cells with ZnT gene disruption and transporter re-expression; TNAP activation
    exposure
    Genetic deficiency of the two specific secretory ZnT complexes, followed by zinc supplementation in culture; amount unreported in abstract.
    limitations
    Primary abstract-level evidence in engineered chicken DT40 cells with transporter complementation. Not a human dietary deficiency or supplementation trial; assay exposure amounts and mutant-specific residue effects are not inferred.
    nutrient_topic
    Zinc research collection; topical membership is not evidence of a direct dietary effect. · Zinc
    organism
    Gallus gallus
    plain_language
    More available zinc did not bypass missing enzyme-loading machinery.
    primary_references
    [zinc-enz-znt-tnap2011] Tissue nonspecific alkaline phosphatase is activated via a two-step mechanism by zinc transport complexes in the early secretory pathway. (2011). https://pubmed.ncbi.nlm.nih.gov/21402707/ DOI: 10.1074/jbc.m111.227173
    tissue_or_cell_type
    Chicken DT40 early secretory pathway
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    Zinc: transport, enzyme loading, deficiency and nutrient interactions (2026-09-17) · lines 781–792

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Engineered chicken DT40 cells with ZnT gene disruption and transporter re-expression; TNAP activation · source_derived_draft · unverified_draft

    ### zinc-enz-zinc-cannot-bypass-znt-loss Extracellular zinc supplementation did not restore reduced TNAP activity in DT40 cells deficient in both ZnT5-ZnT6 and ZnT7 complexes. Condition category: machinery_impairment nutrient_topic: Zinc research collection; topical membership is not evidence of a direct dietary effect. plain_language: More available zinc did not bypass missing enzyme-loading machinery. organism: Gallus gallus tissue_or_cell_type: Chicken DT40 early secretory pathway experimental_model: Engineered chicken DT40 cells with ZnT gene disruption and transporter re-expression; TNAP activation limitations: Primary abstract-level evidence in engineered chicken DT40 cells with transporter complementation. Not a human dietary deficiency or supplementation trial; assay exposure amounts and mutant-specific residue effects are not inferred. exposure: Genetic deficiency of the two specific secretory ZnT complexes, followed by zinc supplementation in culture; amount unreported in abstract. cross_nutrient: false [zinc-enz-znt-tnap2011] Tissue nonspecific alkaline phosphatase is activated via a two-step mechanism by zinc transport complexes in the early secretory pathway. (2011). https://pubmed.ncbi.nlm.nih.gov/21402707/ DOI: 10.1074/jbc.m111.227173
    Complete structured claim and evidence

  2. Reconstitution of ZnT5-ZnT6 with transport-incompetent ZnT5 did not restore TNAP activity.

    Transport-incompetent human ZnT5 study state → Tissue-nonspecific alkaline phosphatase ALPL / TNAP source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    cross_nutrient
    false
    experimental_model
    Engineered chicken DT40 cells with ZnT gene disruption and transporter re-expression; TNAP activation
    exposure
    Transport-incompetent ZnT5 variant with ZnT6, compared with functional loading machinery.
    limitations
    Primary abstract-level evidence in engineered chicken DT40 cells with transporter complementation. Not a human dietary deficiency or supplementation trial; assay exposure amounts and mutant-specific residue effects are not inferred.
    nutrient_topic
    Zinc research collection; topical membership is not evidence of a direct dietary effect. · Zinc
    organism
    Gallus gallus cell model with human proteins
    plain_language
    Protecting the enzyme protein is insufficient when the complex cannot deliver zinc.
    primary_references
    [zinc-enz-znt-tnap2011] Tissue nonspecific alkaline phosphatase is activated via a two-step mechanism by zinc transport complexes in the early secretory pathway. (2011). https://pubmed.ncbi.nlm.nih.gov/21402707/ DOI: 10.1074/jbc.m111.227173
    tissue_or_cell_type
    Chicken DT40 early secretory pathway
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    Zinc: transport, enzyme loading, deficiency and nutrient interactions (2026-09-17) · lines 807–818

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Engineered chicken DT40 cells with ZnT gene disruption and transporter re-expression; TNAP activation · source_derived_draft · unverified_draft

    ### zinc-enz-znt-mutant-no-activity Reconstitution of ZnT5-ZnT6 with transport-incompetent ZnT5 did not restore TNAP activity. Condition category: machinery_impairment nutrient_topic: Zinc research collection; topical membership is not evidence of a direct dietary effect. plain_language: Protecting the enzyme protein is insufficient when the complex cannot deliver zinc. organism: Gallus gallus cell model with human proteins tissue_or_cell_type: Chicken DT40 early secretory pathway experimental_model: Engineered chicken DT40 cells with ZnT gene disruption and transporter re-expression; TNAP activation limitations: Primary abstract-level evidence in engineered chicken DT40 cells with transporter complementation. Not a human dietary deficiency or supplementation trial; assay exposure amounts and mutant-specific residue effects are not inferred. exposure: Transport-incompetent ZnT5 variant with ZnT6, compared with functional loading machinery. cross_nutrient: false [zinc-enz-znt-tnap2011] Tissue nonspecific alkaline phosphatase is activated via a two-step mechanism by zinc transport complexes in the early secretory pathway. (2011). https://pubmed.ncbi.nlm.nih.gov/21402707/ DOI: 10.1074/jbc.m111.227173
    Complete structured claim and evidence

  3. A transport-incompetent ZnT5 variant expressed with ZnT6 stabilized TNAP protein as the apo form despite failing to restore enzyme activity.

    Transport-incompetent human ZnT5 study state → Tissue-nonspecific alkaline phosphatase ALPL / TNAP source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    cross_nutrient
    false
    experimental_model
    Engineered chicken DT40 cells with ZnT gene disruption and transporter re-expression; TNAP activation
    exposure
    Transport-incompetent ZnT5 variant reconstituted with ZnT6 in DT40 cells.
    limitations
    Primary abstract-level evidence in engineered chicken DT40 cells with transporter complementation. Not a human dietary deficiency or supplementation trial; assay exposure amounts and mutant-specific residue effects are not inferred.
    nutrient_topic
    Zinc research collection; topical membership is not evidence of a direct dietary effect. · Zinc
    organism
    Gallus gallus cell model with human proteins
    plain_language
    The transporter complex can protect the unfinished protein even when zinc transport fails.
    primary_references
    [zinc-enz-znt-tnap2011] Tissue nonspecific alkaline phosphatase is activated via a two-step mechanism by zinc transport complexes in the early secretory pathway. (2011). https://pubmed.ncbi.nlm.nih.gov/21402707/ DOI: 10.1074/jbc.m111.227173
    tissue_or_cell_type
    Chicken DT40 early secretory pathway; human transporter complementation
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    Zinc: transport, enzyme loading, deficiency and nutrient interactions (2026-09-17) · lines 794–805

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Engineered chicken DT40 cells with ZnT gene disruption and transporter re-expression; TNAP activation · source_derived_draft · unverified_draft

    ### zinc-enz-znt-mutant-stabilizes A transport-incompetent ZnT5 variant expressed with ZnT6 stabilized TNAP protein as the apo form despite failing to restore enzyme activity. Condition category: machinery_impairment nutrient_topic: Zinc research collection; topical membership is not evidence of a direct dietary effect. plain_language: The transporter complex can protect the unfinished protein even when zinc transport fails. organism: Gallus gallus cell model with human proteins tissue_or_cell_type: Chicken DT40 early secretory pathway; human transporter complementation experimental_model: Engineered chicken DT40 cells with ZnT gene disruption and transporter re-expression; TNAP activation limitations: Primary abstract-level evidence in engineered chicken DT40 cells with transporter complementation. Not a human dietary deficiency or supplementation trial; assay exposure amounts and mutant-specific residue effects are not inferred. exposure: Transport-incompetent ZnT5 variant reconstituted with ZnT6 in DT40 cells. cross_nutrient: false [zinc-enz-znt-tnap2011] Tissue nonspecific alkaline phosphatase is activated via a two-step mechanism by zinc transport complexes in the early secretory pathway. (2011). https://pubmed.ncbi.nlm.nih.gov/21402707/ DOI: 10.1074/jbc.m111.227173
    Complete structured claim and evidence

  4. The ZnT5-ZnT6 and ZnT7 complexes support TNAP conversion from apoenzyme to zinc-loaded active enzyme in the early secretory pathway.

    Human ZnT5-ZnT6 heterodimer → Tissue-nonspecific alkaline phosphatase ALPL / TNAP source_derived_draftungraded
    Experimental context and source evidence
    cross_nutrient
    false
    experimental_model
    Engineered chicken DT40 cells with ZnT gene disruption and transporter re-expression; TNAP activation
    exposure
    ZnT gene disruption and transporter re-expression comparisons.
    limitations
    Primary abstract-level evidence in engineered chicken DT40 cells with transporter complementation. Not a human dietary deficiency or supplementation trial; assay exposure amounts and mutant-specific residue effects are not inferred.
    nutrient_topic
    Zinc research collection; topical membership is not evidence of a direct dietary effect. · Zinc
    organism
    Gallus gallus cell model with human proteins
    plain_language
    Specific transporter complexes deliver zinc while TNAP matures.
    primary_references
    [zinc-enz-znt-tnap2011] Tissue nonspecific alkaline phosphatase is activated via a two-step mechanism by zinc transport complexes in the early secretory pathway. (2011). https://pubmed.ncbi.nlm.nih.gov/21402707/ DOI: 10.1074/jbc.m111.227173
    tissue_or_cell_type
    Chicken DT40 early secretory pathway; human transporter complementation

    Zinc: transport, enzyme loading, deficiency and nutrient interactions (2026-09-17) · lines 768–779

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Engineered chicken DT40 cells with ZnT gene disruption and transporter re-expression; TNAP activation · source_derived_draft · unverified_draft

    ### zinc-enz-znt-specific-maturation The ZnT5-ZnT6 and ZnT7 complexes support TNAP conversion from apoenzyme to zinc-loaded active enzyme in the early secretory pathway. Condition category: normal nutrient_topic: Zinc research collection; topical membership is not evidence of a direct dietary effect. plain_language: Specific transporter complexes deliver zinc while TNAP matures. organism: Gallus gallus cell model with human proteins tissue_or_cell_type: Chicken DT40 early secretory pathway; human transporter complementation experimental_model: Engineered chicken DT40 cells with ZnT gene disruption and transporter re-expression; TNAP activation limitations: Primary abstract-level evidence in engineered chicken DT40 cells with transporter complementation. Not a human dietary deficiency or supplementation trial; assay exposure amounts and mutant-specific residue effects are not inferred. exposure: ZnT gene disruption and transporter re-expression comparisons. cross_nutrient: false [zinc-enz-znt-tnap2011] Tissue nonspecific alkaline phosphatase is activated via a two-step mechanism by zinc transport complexes in the early secretory pathway. (2011). https://pubmed.ncbi.nlm.nih.gov/21402707/ DOI: 10.1074/jbc.m111.227173
    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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