Component

Human protein kinase CK2 complex

Human protein kinase CK2 complex; model and exposure are recorded in linked claims.

3 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. The study identified CK2-dependent phosphorylation of ZIP7 as a regulatory step preceding cytosolic zinc release from intracellular stores.

    Human protein kinase CK2 complex → Human zinc transporter ZIP7 / SLC39A7 source_derived_draftungraded
    Experimental context and source evidence
    cross_nutrient
    ZIP7 phosphorylation (regulatory_event); Zinc(II) ion (transported_ion)
    evidence_span
    {"source_cache": "artifacts/zinc-signaling-sources/22317921-abstract.txt", "locator": "Primary indexed abstract", "file_sha256": "a8e31db38c22019d7ebef8ff165e2b3dc0b3a338e18514f0bf0c48cc5215944d"}
    experimental_model
    Human breast-cell model with ZIP7/CK2 perturbations
    exposure
    Signaling stimuli and ZIP7/CK2 phosphorylation comparisons.
    limitations
    Cellular signaling study; it does not establish dietary zinc supplementation as an anticancer intervention. Intracellular release is different from net dietary uptake.
    nutrient_topic
    Zinc research collection; topical membership is not evidence of a direct dietary effect. · Zinc
    organism
    Homo sapiens
    plain_language
    A kinase can open the route from stored zinc to a cytoplasmic signal.
    primary_references
    [zn-sig-22317921] Protein kinase CK2 triggers cytosolic zinc signaling pathways by phosphorylation of zinc channel ZIP7. (2012). https://pubmed.ncbi.nlm.nih.gov/22317921/ DOI: 10.1126/scisignal.2002585
    tissue_or_cell_type
    Endoplasmic reticulum and cytoplasm

    Zinc: transport, enzyme loading, deficiency and nutrient interactions (2026-09-17) · lines 985–997

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human breast-cell model with ZIP7/CK2 perturbations · source_derived_draft · unverified_draft

    ### zn-sig-ck2-zip7 The study identified CK2-dependent phosphorylation of ZIP7 as a regulatory step preceding cytosolic zinc release from intracellular stores. Condition category: normal nutrient_topic: Zinc research collection; topical membership is not evidence of a direct dietary effect. plain_language: A kinase can open the route from stored zinc to a cytoplasmic signal. organism: Homo sapiens tissue_or_cell_type: Endoplasmic reticulum and cytoplasm experimental_model: Human breast-cell model with ZIP7/CK2 perturbations limitations: Cellular signaling study; it does not establish dietary zinc supplementation as an anticancer intervention. Intracellular release is different from net dietary uptake. exposure: Signaling stimuli and ZIP7/CK2 phosphorylation comparisons. cross_nutrient: ZIP7 phosphorylation (regulatory_event); Zinc(II) ion (transported_ion) evidence_span: {"source_cache": "artifacts/zinc-signaling-sources/22317921-abstract.txt", "locator": "Primary indexed abstract", "file_sha256": "a8e31db38c22019d7ebef8ff165e2b3dc0b3a338e18514f0bf0c48cc5215944d"} [zn-sig-22317921] Protein kinase CK2 triggers cytosolic zinc signaling pathways by phosphorylation of zinc channel ZIP7. (2012). https://pubmed.ncbi.nlm.nih.gov/22317921/ DOI: 10.1126/scisignal.2002585
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. LPS reduced carrier-mediated biotin uptake in NCM460 cells; CK2 inhibition and a putative CK2-site SMVT mutant supported a CK2-related trafficking mechanism.

    Lipopolysaccharide → Human colonic epithelial biotin uptake source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    evidence_span
    {"source_cache": "artifacts/biotin-research/28052864.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "2f27f27a7730837eff6529a7eccf67b3587df28af01ac0507d1b692410483703", "start_char": 0, "end_char": 1549, "text_sha256": "2f27f27a7730837eff6529a7eccf67b3587df28af01ac0507d1b692410483703"}
    experimental_model
    LPS exposure of human NCM460 cells with separate mouse experiments
    exposure
    LPS, CK2 inhibitors and SMVT Thr78Ala mutation
    limitations
    CK2 involvement is supported experimentally but the full causal sequence remains qualified; whole-body human deficiency was not measured.
    nutrient_topic
    Biotin research collection; topical membership is not evidence of a direct dietary effect. · Biotin
    organism
    Homo sapiens
    plain_language
    Inflammatory exposure interfered with biotin entry in this model.
    primary_references
    [b7-p28052864] Lipopolysaccharide inhibits colonic biotin uptake via interference with membrane expression of its transporter: a role for a casein kinase 2-mediated pathway. (2017). https://pubmed.ncbi.nlm.nih.gov/28052864/ DOI: 10.1152/ajpcell.00300.2016
    tissue_or_cell_type
    Colonic epithelial NCM460 cells
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    Biotin: carboxylases, recycling, deficiency and nutrient interactions (2026-09-17) · lines 1118–1129

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · LPS exposure of human NCM460 cells with separate mouse experiments · source_derived_draft · unverified_draft

    ### b7-lps-uptake LPS reduced carrier-mediated biotin uptake in NCM460 cells; CK2 inhibition and a putative CK2-site SMVT mutant supported a CK2-related trafficking mechanism. Condition category: machinery_impairment nutrient_topic: Biotin research collection; topical membership is not evidence of a direct dietary effect. plain_language: Inflammatory exposure interfered with biotin entry in this model. organism: Homo sapiens tissue_or_cell_type: Colonic epithelial NCM460 cells experimental_model: LPS exposure of human NCM460 cells with separate mouse experiments limitations: CK2 involvement is supported experimentally but the full causal sequence remains qualified; whole-body human deficiency was not measured. exposure: LPS, CK2 inhibitors and SMVT Thr78Ala mutation evidence_span: {"source_cache": "artifacts/biotin-research/28052864.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "2f27f27a7730837eff6529a7eccf67b3587df28af01ac0507d1b692410483703", "start_char": 0, "end_char": 1549, "text_sha256": "2f27f27a7730837eff6529a7eccf67b3587df28af01ac0507d1b692410483703"} [b7-p28052864] Lipopolysaccharide inhibits colonic biotin uptake via interference with membrane expression of its transporter: a role for a casein kinase 2-mediated pathway. (2017). https://pubmed.ncbi.nlm.nih.gov/28052864/ DOI: 10.1152/ajpcell.00300.2016
    Complete structured claim and evidence

  2. ZIP7 phosphorylation was linked to release of stored zinc and downstream AKT and ERK1/2 phosphorylation in the studied human cells.

    Human zinc transporter ZIP7 / SLC39A7 → Endoplasmic-reticulum zinc release source_derived_draftungraded
    Experimental context and source evidence
    cross_nutrient
    Human protein kinase CK2 complex (upstream_kinase); AKT serine/threonine kinase family (downstream_kinase_family); Human ERK2 / MAPK1 (downstream_kinase); Human ERK1 / MAPK3 (downstream_kinase); Cytosolic labile zinc availability (increased_pool)
    evidence_span
    {"source_cache": "artifacts/zinc-signaling-sources/22317921-abstract.txt", "locator": "Primary indexed abstract", "file_sha256": "a8e31db38c22019d7ebef8ff165e2b3dc0b3a338e18514f0bf0c48cc5215944d"}
    experimental_model
    Human breast-cell model with ZIP7/CK2 perturbations
    exposure
    Signaling stimuli and ZIP7/CK2 phosphorylation comparisons.
    limitations
    Cellular signaling study; it does not establish dietary zinc supplementation as an anticancer intervention. Intracellular release is different from net dietary uptake.
    nutrient_topic
    Zinc research collection; topical membership is not evidence of a direct dietary effect. · Zinc
    organism
    Homo sapiens
    plain_language
    Zinc redistribution connected a storage compartment to kinase signaling.
    primary_references
    [zn-sig-22317921] Protein kinase CK2 triggers cytosolic zinc signaling pathways by phosphorylation of zinc channel ZIP7. (2012). https://pubmed.ncbi.nlm.nih.gov/22317921/ DOI: 10.1126/scisignal.2002585
    tissue_or_cell_type
    Endoplasmic reticulum and cytoplasm

    Zinc: transport, enzyme loading, deficiency and nutrient interactions (2026-09-17) · lines 999–1011

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human breast-cell model with ZIP7/CK2 perturbations · source_derived_draft · unverified_draft

    ### zn-sig-zip7-release ZIP7 phosphorylation was linked to release of stored zinc and downstream AKT and ERK1/2 phosphorylation in the studied human cells. Condition category: normal nutrient_topic: Zinc research collection; topical membership is not evidence of a direct dietary effect. plain_language: Zinc redistribution connected a storage compartment to kinase signaling. organism: Homo sapiens tissue_or_cell_type: Endoplasmic reticulum and cytoplasm experimental_model: Human breast-cell model with ZIP7/CK2 perturbations limitations: Cellular signaling study; it does not establish dietary zinc supplementation as an anticancer intervention. Intracellular release is different from net dietary uptake. exposure: Signaling stimuli and ZIP7/CK2 phosphorylation comparisons. cross_nutrient: Human protein kinase CK2 complex (upstream_kinase); AKT serine/threonine kinase family (downstream_kinase_family); Human ERK2 / MAPK1 (downstream_kinase); Human ERK1 / MAPK3 (downstream_kinase); Cytosolic labile zinc availability (increased_pool) evidence_span: {"source_cache": "artifacts/zinc-signaling-sources/22317921-abstract.txt", "locator": "Primary indexed abstract", "file_sha256": "a8e31db38c22019d7ebef8ff165e2b3dc0b3a338e18514f0bf0c48cc5215944d"} [zn-sig-22317921] Protein kinase CK2 triggers cytosolic zinc signaling pathways by phosphorylation of zinc channel ZIP7. (2012). https://pubmed.ncbi.nlm.nih.gov/22317921/ DOI: 10.1126/scisignal.2002585
    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