Component

Nucleus

Cellular compartment containing genomic DNA.

5 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. The newly characterized 700-amino-acid PIP5K1C_i4 isoform localized to the nucleus.

    Human PIP5K1C_i4 isoform (700 amino acids) → Nucleus source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/inositol-research/19548880.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "5ae150d47bf139d7352c8a5a128e0d6b071340f8c47d78700d5f398a549d3cd8", "start_char": 0, "end_char": 1766, "text_sha256": "5ae150d47bf139d7352c8a5a128e0d6b071340f8c47d78700d5f398a549d3cd8"}
    experimental_model
    Human splice-isoform expression, localization and kinase assay
    exposure
    PIP5K1C_i4 and i5 characterization
    limitations
    Isoforms have different localizations; a bulk lipid concentration cannot describe every local pool.
    nutrient_topic
    Inositol research collection; topical membership is not evidence of a direct dietary effect. · Inositol (stereoisomer family)
    organism
    Human proteins in cellular expression assays
    plain_language
    Where an enzyme works can matter as much as its reaction.
    primary_references
    [ino-p19548880] Two novel phosphatidylinositol-4-phosphate 5-kinase type Igamma splice variants expressed in human cells display distinctive cellular targeting. (2009). https://pubmed.ncbi.nlm.nih.gov/19548880/ DOI: 10.1042/bj20090638
    tissue_or_cell_type
    Nuclear and vesicular compartments

    Inositol: synthesis, signaling, mineral interactions and conditional deficiency (2026-09-17) · lines 600–611

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human splice-isoform expression, localization and kinase assay · source_derived_draft · unverified_draft

    ### ino-pip5k-i4-location The newly characterized 700-amino-acid PIP5K1C_i4 isoform localized to the nucleus. Condition category: normal nutrient_topic: Inositol research collection; topical membership is not evidence of a direct dietary effect. plain_language: Where an enzyme works can matter as much as its reaction. organism: Human proteins in cellular expression assays tissue_or_cell_type: Nuclear and vesicular compartments experimental_model: Human splice-isoform expression, localization and kinase assay limitations: Isoforms have different localizations; a bulk lipid concentration cannot describe every local pool. exposure: PIP5K1C_i4 and i5 characterization evidence_span: {"source_cache": "artifacts/inositol-research/19548880.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "5ae150d47bf139d7352c8a5a128e0d6b071340f8c47d78700d5f398a549d3cd8", "start_char": 0, "end_char": 1766, "text_sha256": "5ae150d47bf139d7352c8a5a128e0d6b071340f8c47d78700d5f398a549d3cd8"} [ino-p19548880] Two novel phosphatidylinositol-4-phosphate 5-kinase type Igamma splice variants expressed in human cells display distinctive cellular targeting. (2009). https://pubmed.ncbi.nlm.nih.gov/19548880/ DOI: 10.1042/bj20090638
    Complete structured claim and evidence

  2. Dietary folate depletion increased nuclear Mthfd1 more than twofold in mouse liver at the expense of cytosolic levels.

    Mouse Mthfd1 protein → Nucleus source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    nutrient_deficiency Imported condition classification; unverified.
    experimental_model
    Dietary depletion and liver fractionation
    exposure
    Assay conditions described in the linked primary study.
    limitations
    Nuclear protection is conditional; it does not prove indefinite resistance to deficiency.
    nutrient_topic
    Folate and folic acid research collection; topical membership is not evidence of a direct dietary effect. · Folate (vitamin B9)
    organism
    Mus musculus
    plain_language
    The enzyme redistributed toward the nucleus as folate supply fell.
    primary_references
    [field-2014] Nuclear enrichment of folate cofactors and methylenetetrahydrofolate dehydrogenase 1 (MTHFD1) protect de novo thymidylate biosynthesis during folate deficiency (2014). https://pubmed.ncbi.nlm.nih.gov/25213861/ DOI: 10.1074/jbc.m114.599589
    tissue_or_cell_type
    Liver
    trigger_kind
    nutrient_deficiency Imported condition classification; unverified.

    Folate and folic acid: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 961–971

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Dietary depletion and liver fractionation · source_derived_draft · unverified_draft

    ### mouse-folate-depletion-mthfd1-enrichment Dietary folate depletion increased nuclear Mthfd1 more than twofold in mouse liver at the expense of cytosolic levels. Condition category: nutrient_deficiency nutrient_topic: Folate and folic acid research collection; topical membership is not evidence of a direct dietary effect. plain_language: The enzyme redistributed toward the nucleus as folate supply fell. organism: Mus musculus tissue_or_cell_type: Liver experimental_model: Dietary depletion and liver fractionation limitations: Nuclear protection is conditional; it does not prove indefinite resistance to deficiency. exposure: Assay conditions described in the linked primary study. [field-2014] Nuclear enrichment of folate cofactors and methylenetetrahydrofolate dehydrogenase 1 (MTHFD1) protect de novo thymidylate biosynthesis during folate deficiency (2014). https://pubmed.ncbi.nlm.nih.gov/25213861/ DOI: 10.1074/jbc.m114.599589
    Complete structured claim and evidence

  3. Nuclear folate levels resisted depletion despite more than 50% lower total cellular folate in folate-depleted mouse liver.

    Folate (vitamin B9) → Nucleus source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    nutrient_deficiency Imported condition classification; unverified.
    experimental_model
    Dietary depletion and liver fractionation
    exposure
    Assay conditions described in the linked primary study.
    limitations
    Nuclear protection is conditional; it does not prove indefinite resistance to deficiency.
    nutrient_topic
    Folate and folic acid research collection; topical membership is not evidence of a direct dietary effect. · Folate (vitamin B9)
    organism
    Mus musculus
    plain_language
    The nucleus retained folate even when whole-cell stores fell.
    primary_references
    [field-2014] Nuclear enrichment of folate cofactors and methylenetetrahydrofolate dehydrogenase 1 (MTHFD1) protect de novo thymidylate biosynthesis during folate deficiency (2014). https://pubmed.ncbi.nlm.nih.gov/25213861/ DOI: 10.1074/jbc.m114.599589
    tissue_or_cell_type
    Liver
    trigger_kind
    nutrient_deficiency Imported condition classification; unverified.

    Folate and folic acid: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 1347–1357

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Dietary depletion and liver fractionation · source_derived_draft · unverified_draft

    ### mouse-folate-depletion-nuclear-retention Nuclear folate levels resisted depletion despite more than 50% lower total cellular folate in folate-depleted mouse liver. Condition category: nutrient_deficiency nutrient_topic: Folate and folic acid research collection; topical membership is not evidence of a direct dietary effect. plain_language: The nucleus retained folate even when whole-cell stores fell. organism: Mus musculus tissue_or_cell_type: Liver experimental_model: Dietary depletion and liver fractionation limitations: Nuclear protection is conditional; it does not prove indefinite resistance to deficiency. exposure: Assay conditions described in the linked primary study. [field-2014] Nuclear enrichment of folate cofactors and methylenetetrahydrofolate dehydrogenase 1 (MTHFD1) protect de novo thymidylate biosynthesis during folate deficiency (2014). https://pubmed.ncbi.nlm.nih.gov/25213861/ DOI: 10.1074/jbc.m114.599589
    Complete structured claim and evidence

  4. MTHFD1 accumulated in nuclei of S-phase HeLa and MCF7 cells.

    Human MTHFD1 → Nucleus source_derived_draftungraded
    Experimental context and source evidence
    experimental_model
    Cell-cycle localization experiments
    exposure
    Assay conditions described in the linked primary study.
    limitations
    Cultured-cell localization; not a whole-body folate biomarker.
    nutrient_topic
    Folate and folic acid research collection; topical membership is not evidence of a direct dietary effect. · Folate (vitamin B9)
    organism
    Homo sapiens
    plain_language
    The enzyme moves toward the compartment where DNA is copied.
    primary_references
    [field-2014] Nuclear enrichment of folate cofactors and methylenetetrahydrofolate dehydrogenase 1 (MTHFD1) protect de novo thymidylate biosynthesis during folate deficiency (2014). https://pubmed.ncbi.nlm.nih.gov/25213861/ DOI: 10.1074/jbc.m114.599589
    tissue_or_cell_type
    HeLa and MCF7 cells

    Folate and folic acid: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 949–959

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Cell-cycle localization experiments · source_derived_draft · unverified_draft

    ### mthfd1-s-phase-localization MTHFD1 accumulated in nuclei of S-phase HeLa and MCF7 cells. Condition category: normal nutrient_topic: Folate and folic acid research collection; topical membership is not evidence of a direct dietary effect. plain_language: The enzyme moves toward the compartment where DNA is copied. organism: Homo sapiens tissue_or_cell_type: HeLa and MCF7 cells experimental_model: Cell-cycle localization experiments limitations: Cultured-cell localization; not a whole-body folate biomarker. exposure: Assay conditions described in the linked primary study. [field-2014] Nuclear enrichment of folate cofactors and methylenetetrahydrofolate dehydrogenase 1 (MTHFD1) protect de novo thymidylate biosynthesis during folate deficiency (2014). https://pubmed.ncbi.nlm.nih.gov/25213861/ DOI: 10.1074/jbc.m114.599589
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. Calcineurin binds NFAT1 and supports its reversible dephosphorylated, nuclear-active state during calcium stimulation.

    Calcineurin → NFAT1 / NFATC2 source_derived_draftungraded
    Experimental context and source evidence
    compartment_description
    Cytosol and nucleus
    experimental_model
    Murine T-cell experiments, inhibitor/chelation interventions and protein-binding assays
    limitations
    NFAT1-specific evidence; do not assign this calcium response to all NFAT proteins or NFAT5.
    nutrient_topic
    Calcium research collection; topical membership is not evidence of a direct dietary effect. · Calcium
    organism
    Mus musculus
    plain_language
    Calcineurin connects calcium signaling to NFAT1 activation.
    primary_references
    [ca-loh1996] Calcineurin binds the transcription factor NFAT1 and reversibly regulates its activity (1996). https://pubmed.ncbi.nlm.nih.gov/8631904/ DOI: 10.1074/jbc.271.18.10884
    research_relationship_category
    regulation
    tissue_or_cell_type
    T lymphocytes

    Calcium: mechanism-first literature curation (2026-09-17) · lines 425–436

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Murine T-cell experiments, inhibitor/chelation interventions and protein-binding assays · source_derived_draft · unverified_draft

    ### ca-calcineurin-nfat1-regulation Calcineurin binds NFAT1 and supports its reversible dephosphorylated, nuclear-active state during calcium stimulation. Condition category: normal nutrient_topic: Calcium research collection; topical membership is not evidence of a direct dietary effect. plain_language: Calcineurin connects calcium signaling to NFAT1 activation. organism: Mus musculus tissue_or_cell_type: T lymphocytes experimental_model: Murine T-cell experiments, inhibitor/chelation interventions and protein-binding assays limitations: NFAT1-specific evidence; do not assign this calcium response to all NFAT proteins or NFAT5. research_relationship_category: regulation compartment_description: Cytosol and nucleus [ca-loh1996] Calcineurin binds the transcription factor NFAT1 and reversibly regulates its activity (1996). https://pubmed.ncbi.nlm.nih.gov/8631904/ DOI: 10.1074/jbc.271.18.10884
    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