Component

Nuclear receptor coactivator 2 / TIF2

Nuclear receptor coactivator 2 / TIF2; specific protein identity, with organism and perturbation supplied in each claim.

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 acts on it

  1. DIM promoted ERbeta recruitment of SRC-2 at regulatory elements; SRC-2 silencing inhibited target-gene activation.

    3,3'-Diindolylmethane / DIM → Nuclear receptor coactivator 2 / TIF2 source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/dim-research/20160136.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "558ee877330aede2675ccccdef5e31debf9824e00a1eaaacb1e7fe385d45b8e5", "start_char": 0, "end_char": 1134, "text_sha256": "558ee877330aede2675ccccdef5e31debf9824e00a1eaaacb1e7fe385d45b8e5"}
    experimental_model
    Reporter, binding, chromatin and coactivator-silencing assays
    exposure
    DIM and SRC-2 silencing
    limitations
    Subtype-selective response in this system; other studies find ERalpha responses under other hormonal and concentration conditions.
    nutrient_topic
    Diindolylmethane (DIM) research collection; topical membership is not evidence of a direct dietary effect. · 3,3'-Diindolylmethane / DIM
    organism
    Human receptor-expressing cell systems
    plain_language
    A separate coactivator was required for the transcriptional response.
    primary_references
    [dim-p20160136] Selective activation of estrogen receptor-beta target genes by 3,3'-diindolylmethane. (2010). https://pubmed.ncbi.nlm.nih.gov/20160136/ DOI: 10.1210/en.2009-1028
    tissue_or_cell_type
    ERbeta transcription

    Diindolylmethane (DIM): formation, receptor signaling, metabolism and drug interactions (2026-09-17) · lines 584–595

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Reporter, binding, chromatin and coactivator-silencing assays · source_derived_draft · unverified_draft

    ### dim-src2-recruitment DIM promoted ERbeta recruitment of SRC-2 at regulatory elements; SRC-2 silencing inhibited target-gene activation. Condition category: normal nutrient_topic: Diindolylmethane (DIM) research collection; topical membership is not evidence of a direct dietary effect. plain_language: A separate coactivator was required for the transcriptional response. organism: Human receptor-expressing cell systems tissue_or_cell_type: ERbeta transcription experimental_model: Reporter, binding, chromatin and coactivator-silencing assays limitations: Subtype-selective response in this system; other studies find ERalpha responses under other hormonal and concentration conditions. exposure: DIM and SRC-2 silencing evidence_span: {"source_cache": "artifacts/dim-research/20160136.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "558ee877330aede2675ccccdef5e31debf9824e00a1eaaacb1e7fe385d45b8e5", "start_char": 0, "end_char": 1134, "text_sha256": "558ee877330aede2675ccccdef5e31debf9824e00a1eaaacb1e7fe385d45b8e5"} [dim-p20160136] Selective activation of estrogen receptor-beta target genes by 3,3'-diindolylmethane. (2010). https://pubmed.ncbi.nlm.nih.gov/20160136/ DOI: 10.1210/en.2009-1028
    Complete structured claim and evidence

  2. The agonist-bound RAR ligand-binding domain interacted with TIF2 in an AF-2-dependent manner.

    Retinoic acid receptor alpha → Nuclear receptor coactivator 2 / TIF2 source_derived_draftungraded
    Experimental context and source evidence
    evidence_locator
    Abstract
    experimental_model
    Human TIF2 cloning; in vitro receptor-domain interactions and cellular reporters.
    exposure
    Agonist versus control; AF-2 mutants
    limitations
    Domain assays do not resolve every endogenous chromatin complex.
    nutrient_topic
    Vitamin A research collection; topical membership is not evidence of a direct dietary effect. · Vitamin A
    organism
    Human TIF2 and engineered receptor domains
    plain_language
    An activated receptor gains a binding surface for a transcriptional coactivator.
    primary_references
    [va-voegel-1996] TIF2, a 160 kDa transcriptional mediator for the ligand-dependent activation function AF-2 of nuclear receptors (1996). https://pubmed.ncbi.nlm.nih.gov/8670870/ DOI: 10.1002/j.1460-2075.1996.tb00736.x
    tissue_or_cell_type
    Cell-free and cellular interaction assays

    Vitamin A: forms, mechanisms, deficiency and excess (2026-09-17) · lines 1162–1173

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human TIF2 cloning; in vitro receptor-domain interactions and cellular reporters. · source_derived_draft · unverified_draft

    ### va-sig-rara-tif2-recruitment The agonist-bound RAR ligand-binding domain interacted with TIF2 in an AF-2-dependent manner. Condition category: normal nutrient_topic: Vitamin A research collection; topical membership is not evidence of a direct dietary effect. plain_language: An activated receptor gains a binding surface for a transcriptional coactivator. organism: Human TIF2 and engineered receptor domains tissue_or_cell_type: Cell-free and cellular interaction assays experimental_model: Human TIF2 cloning; in vitro receptor-domain interactions and cellular reporters. limitations: Domain assays do not resolve every endogenous chromatin complex. evidence_locator: Abstract exposure: Agonist versus control; AF-2 mutants [va-voegel-1996] TIF2, a 160 kDa transcriptional mediator for the ligand-dependent activation function AF-2 of nuclear receptors (1996). https://pubmed.ncbi.nlm.nih.gov/8670870/ DOI: 10.1002/j.1460-2075.1996.tb00736.x
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. T3 was bound within the human THRB ligand-binding domain in the crystallized THRB–RXRA domain heterodimer, with the THRB activation surface accommodating an SRC-2-derived peptide.

    T3 → Human THRB ligand-binding domain 202–461 source_derived_draftungraded
    Experimental context and source evidence
    cross_nutrient
    An iodine-containing hormone binds THRB in a complex with the retinoid receptor RXRA; no nutritional vitamin A manipulation.
    evidence_locator
    Figure 2a and Results: structural characterization; Methods: protein production and crystallography
    evidence_spans
    [{"source_document": "artifacts/iodine-metabolism-sources/26289479.txt", "locator": "Figure 2a and Results: structural characterization; Methods: protein production and crystallography", "start_char": 10702, "end_char": 12152}]
    experimental_model
    Human TR beta/RXR alpha ligand-binding-domain crystallography; full-length human receptors in CV-1 reporter assays
    exposure
    Human THRB residues 202–461 and RXRA residues 223–462; threefold molar excess of T3 and synthetic HKILHRLL SRC-2 peptide; structure refined at anisotropic 3.2–3.8 angstrom resolution.
    limitations
    Isolated domains and an eight-residue peptide, not full-length coactivator recruitment in tissue. The structure establishes binding geometry, not a physiological T3 threshold.
    nutrient_topic
    Iodine research collection; topical membership is not evidence of a direct dietary effect. · Iodine
    organism
    Human receptor domains produced in Escherichia coli; synthetic coactivator peptide
    plain_language
    T3 physically occupies its receptor, which presents a docking surface for a transcription coactivator.
    primary_references
    [i-met-26289479] Structural mechanism for signal transduction in RXR nuclear receptor heterodimers. (2015). https://pubmed.ncbi.nlm.nih.gov/26289479/ DOI: 10.1038/ncomms9013
    tissue_or_cell_type
    Purified receptor-domain complex

    Iodine: thyroid hormone production, deficiency, excess and nutrient interactions (2026-09-17) · lines 1172–1185

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human TR beta/RXR alpha ligand-binding-domain crystallography; full-length human receptors in CV-1 reporter assays · source_derived_draft · unverified_draft

    ### i-met-t3-thrb-ligand-binding T3 was bound within the human THRB ligand-binding domain in the crystallized THRB–RXRA domain heterodimer, with the THRB activation surface accommodating an SRC-2-derived peptide. Condition category: normal nutrient_topic: Iodine research collection; topical membership is not evidence of a direct dietary effect. plain_language: T3 physically occupies its receptor, which presents a docking surface for a transcription coactivator. organism: Human receptor domains produced in Escherichia coli; synthetic coactivator peptide tissue_or_cell_type: Purified receptor-domain complex experimental_model: Human TR beta/RXR alpha ligand-binding-domain crystallography; full-length human receptors in CV-1 reporter assays limitations: Isolated domains and an eight-residue peptide, not full-length coactivator recruitment in tissue. The structure establishes binding geometry, not a physiological T3 threshold. exposure: Human THRB residues 202–461 and RXRA residues 223–462; threefold molar excess of T3 and synthetic HKILHRLL SRC-2 peptide; structure refined at anisotropic 3.2–3.8 angstrom resolution. cross_nutrient: An iodine-containing hormone binds THRB in a complex with the retinoid receptor RXRA; no nutritional vitamin A manipulation. evidence_locator: Figure 2a and Results: structural characterization; Methods: protein production and crystallography evidence_spans: [{"source_document": "artifacts/iodine-metabolism-sources/26289479.txt", "locator": "Figure 2a and Results: structural characterization; Methods: protein production and crystallography", "start_char": 10702, "end_char": 12152}] [i-met-26289479] Structural mechanism for signal transduction in RXR nuclear receptor heterodimers. (2015). https://pubmed.ncbi.nlm.nih.gov/26289479/ DOI: 10.1038/ncomms9013
    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