Component

Calcium/calmodulin

The calcium-bound calmodulin complex that activates calcineurin.

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 it acts on

  1. Calcium/calmodulin binding folds the human calcineurin regulatory region and supports displacement of autoinhibition.

    Calcium/calmodulin → Calcineurin source_derived_draftungraded
    Experimental context and source evidence
    compartment_description
    Cytosol
    experimental_model
    Recombinant human alpha-calcineurin, regulatory fragments and calmodulin; spectroscopy and exchange mass spectrometry
    limitations
    Fragment and biochemical data support a regulatory mechanism; not tissue-level output.
    nutrient_topic
    Calcium research collection; topical membership is not evidence of a direct dietary effect. · Calcium
    organism
    Homo sapiens
    plain_language
    Calcium-bound calmodulin helps switch on calcineurin.
    primary_references
    [ca-rumimasante2012] Structural basis for activation of calcineurin by calmodulin (2012). https://pubmed.ncbi.nlm.nih.gov/22100452/ DOI: 10.1016/j.jmb.2011.11.008
    research_relationship_category
    regulation
    tissue_or_cell_type
    Recombinant signaling proteins

    Calcium: mechanism-first literature curation (2026-09-17) · lines 412–423

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Recombinant human alpha-calcineurin, regulatory fragments and calmodulin; spectroscopy and exchange mass spectrometry · source_derived_draft · unverified_draft

    ### ca-calmodulin-calcineurin-activation Calcium/calmodulin binding folds the human calcineurin regulatory region and supports displacement of autoinhibition. Condition category: normal nutrient_topic: Calcium research collection; topical membership is not evidence of a direct dietary effect. plain_language: Calcium-bound calmodulin helps switch on calcineurin. organism: Homo sapiens tissue_or_cell_type: Recombinant signaling proteins experimental_model: Recombinant human alpha-calcineurin, regulatory fragments and calmodulin; spectroscopy and exchange mass spectrometry limitations: Fragment and biochemical data support a regulatory mechanism; not tissue-level output. research_relationship_category: regulation compartment_description: Cytosol [ca-rumimasante2012] Structural basis for activation of calcineurin by calmodulin (2012). https://pubmed.ncbi.nlm.nih.gov/22100452/ DOI: 10.1016/j.jmb.2011.11.008
    Complete structured claim and evidence

  2. Calmodulin increases apparent calcium affinity and ATPase activity of the erythrocyte calcium pump.

    Calcium/calmodulin → Plasma membrane calcium ATPase family source_derived_draftungraded
    Experimental context and source evidence
    compartment_description
    Plasma membrane
    experimental_model
    Human erythrocyte membrane ghosts with purified human or bovine calmodulin
    limitations
    Membrane ghosts with controlled additions; pump isoforms were not resolved and this is not an intact-cell dose response.
    nutrient_topic
    Calcium research collection; topical membership is not evidence of a direct dietary effect. · Calcium
    organism
    Homo sapiens
    plain_language
    Calmodulin makes the red-cell calcium pump respond more strongly to calcium.
    primary_references
    [ca-roufogalis1980] Regulation by calmodulin of the calcium affinity of the calcium-transport ATPase in human erythrocytes (1980). https://pubmed.ncbi.nlm.nih.gov/6109558/ DOI: 10.1139/o80-126
    research_relationship_category
    regulation
    tissue_or_cell_type
    Erythrocyte membranes

    Calcium: mechanism-first literature curation (2026-09-17) · lines 612–623

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human erythrocyte membrane ghosts with purified human or bovine calmodulin · source_derived_draft · unverified_draft

    ### ca-calmodulin-pmca-affinity Calmodulin increases apparent calcium affinity and ATPase activity of the erythrocyte calcium pump. Condition category: normal nutrient_topic: Calcium research collection; topical membership is not evidence of a direct dietary effect. plain_language: Calmodulin makes the red-cell calcium pump respond more strongly to calcium. organism: Homo sapiens tissue_or_cell_type: Erythrocyte membranes experimental_model: Human erythrocyte membrane ghosts with purified human or bovine calmodulin limitations: Membrane ghosts with controlled additions; pump isoforms were not resolved and this is not an intact-cell dose response. research_relationship_category: regulation compartment_description: Plasma membrane [ca-roufogalis1980] Regulation by calmodulin of the calcium affinity of the calcium-transport ATPase in human erythrocytes (1980). https://pubmed.ncbi.nlm.nih.gov/6109558/ DOI: 10.1139/o80-126
    Complete structured claim and evidence

  3. Calcium/calmodulin stimulates autophosphorylation of purified brain CaMKII.

    Calcium/calmodulin → Ca2+/calmodulin-dependent protein kinase II family source_derived_draftungraded
    Experimental context and source evidence
    compartment_description
    Cytosolic kinase complex
    experimental_model
    Purified mammalian brain CaMKII; phosphorylation and substrate-kinase assays
    limitations
    Brain holoenzyme assay; does not identify every isoform or phosphorylation site.
    nutrient_topic
    Calcium research collection; topical membership is not evidence of a direct dietary effect. · Calcium
    organism
    Mammalia
    plain_language
    Calcium-bound calmodulin starts CaMKII self-phosphorylation.
    primary_references
    [ca-miller1986] Regulation of brain type II Ca2+/calmodulin-dependent protein kinase by autophosphorylation: a Ca2+-triggered molecular switch (1986). https://pubmed.ncbi.nlm.nih.gov/3006921/ DOI: 10.1016/0092-8674(86)90008-5
    research_relationship_category
    regulation
    tissue_or_cell_type
    Brain enzyme preparation

    Calcium: mechanism-first literature curation (2026-09-17) · lines 438–449

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified mammalian brain CaMKII; phosphorylation and substrate-kinase assays · source_derived_draft · unverified_draft

    ### ca-camkii-calmodulin-activation Calcium/calmodulin stimulates autophosphorylation of purified brain CaMKII. Condition category: normal nutrient_topic: Calcium research collection; topical membership is not evidence of a direct dietary effect. plain_language: Calcium-bound calmodulin starts CaMKII self-phosphorylation. organism: Mammalia tissue_or_cell_type: Brain enzyme preparation experimental_model: Purified mammalian brain CaMKII; phosphorylation and substrate-kinase assays limitations: Brain holoenzyme assay; does not identify every isoform or phosphorylation site. research_relationship_category: regulation compartment_description: Cytosolic kinase complex [ca-miller1986] Regulation of brain type II Ca2+/calmodulin-dependent protein kinase by autophosphorylation: a Ca2+-triggered molecular switch (1986). https://pubmed.ncbi.nlm.nih.gov/3006921/ DOI: 10.1016/0092-8674(86)90008-5
    Complete structured claim and evidence

  4. Calcium/calmodulin activates calcineurin.

    Calcium/calmodulin → Calcineurin source_derived_draftsupplied_source_only
    Experimental context and source evidence
    cell_type
    · T cell
    evidence_scope
    Source-derived draft; primary-source verification required
    organism
    · Human

    Selenium in immune cells · lines 30–38

    Selenium immune-cell mechanism draft · supports · Source draft; model details require primary-source verification · source_derived_draft · unverified_draft

    5. TCR → LCK → ZAP70 → LAT → PLCγ1 → PIP₂ → IP₃ + DAG 6. IP₃ → IP3R → ER Ca²⁺ release → store depletion 7. STIM1 oligomerizes → ORAI1 → CRAC channel → sustained Ca²⁺ entry 8. Ca²⁺/calmodulin → CALCINEURIN (PP2B) → dephosphorylates NFAT 9. NFAT → nucleus → partners with AP-1 → IL2, IFNG, CD25 transcription
    Complete structured claim and evidence

What acts on it

  1. Calcium binding forms the calcium/calmodulin signaling complex.

    Calcium ion → Calcium/calmodulin source_derived_draftsupplied_source_only
    Experimental context and source evidence
    cell_type
    · T cell
    evidence_scope
    Source-derived draft; primary-source verification required
    organism
    · Human

    Selenium in immune cells · lines 30–38

    Selenium immune-cell mechanism draft · supports · Source draft; model details require primary-source verification · source_derived_draft · unverified_draft

    5. TCR → LCK → ZAP70 → LAT → PLCγ1 → PIP₂ → IP₃ + DAG 6. IP₃ → IP3R → ER Ca²⁺ release → store depletion 7. STIM1 oligomerizes → ORAI1 → CRAC channel → sustained Ca²⁺ entry 8. Ca²⁺/calmodulin → CALCINEURIN (PP2B) → dephosphorylates NFAT 9. NFAT → nucleus → partners with AP-1 → IL2, IFNG, CD25 transcription
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. Calcium-loaded calmodulin forms the Ca2+/CaM regulatory complex resolved with a myosin-light-chain-kinase target peptide.

    Calcium ion → Calmodulin source_derived_draftungraded
    Experimental context and source evidence
    compartment_description
    Cytosolic protein complex
    experimental_model
    Purified calcium-bound calmodulin and a chicken smooth-muscle myosin light-chain kinase peptide; crystallography
    limitations
    Structure of a peptide complex; not a measurement of dietary calcium effects or every calmodulin target.
    nutrient_topic
    Calcium research collection; topical membership is not evidence of a direct dietary effect. · Calcium
    organism
    Purified vertebrate proteins
    plain_language
    Calmodulin carries bound calcium while engaging a target protein.
    primary_references
    [ca-meador1992] Target enzyme recognition by calmodulin: 2.4 A structure of a calmodulin-peptide complex (1992). https://pubmed.ncbi.nlm.nih.gov/1519061/ DOI: 10.1126/science.1519061
    research_relationship_category
    binding
    tissue_or_cell_type
    Smooth-muscle target-peptide system

    Calcium: mechanism-first literature curation (2026-09-17) · lines 399–410

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified calcium-bound calmodulin and a chicken smooth-muscle myosin light-chain kinase peptide; crystallography · source_derived_draft · unverified_draft

    ### ca-calmodulin-calcium-complex Calcium-loaded calmodulin forms the Ca2+/CaM regulatory complex resolved with a myosin-light-chain-kinase target peptide. Condition category: normal nutrient_topic: Calcium research collection; topical membership is not evidence of a direct dietary effect. plain_language: Calmodulin carries bound calcium while engaging a target protein. organism: Purified vertebrate proteins tissue_or_cell_type: Smooth-muscle target-peptide system experimental_model: Purified calcium-bound calmodulin and a chicken smooth-muscle myosin light-chain kinase peptide; crystallography limitations: Structure of a peptide complex; not a measurement of dietary calcium effects or every calmodulin target. research_relationship_category: binding compartment_description: Cytosolic protein complex [ca-meador1992] Target enzyme recognition by calmodulin: 2.4 A structure of a calmodulin-peptide complex (1992). https://pubmed.ncbi.nlm.nih.gov/1519061/ DOI: 10.1126/science.1519061
    Complete structured claim and evidence

  2. NOS converted arginine to N-hydroxyarginine in an oxygen- and calcium/calmodulin-dependent partial reaction.

    L-Arginine → Nω-Hydroxy-L-arginine source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Rat cerebellar NOS preparation; separated partial reactions.
    limitations
    Purified preparation; residual enzyme reductant supported a limited first reaction without added NADPH. This does not imply physiological NOS is NADPH independent.
    nutrient_topic
    L-Arginine collection; tissue, species, dose and formulation distinctions retained. · L-Arginine
    plain_language
    Nitric-oxide production passes through a distinct intermediate.
    primary_references
    Characteristics of the nitric oxide synthase-catalyzed conversion of arginine to N-hydroxyarginine, the first oxygenation step in the enzymic synthesis of nitric oxide. · 1995 · https://pubmed.ncbi.nlm.nih.gov/7530247/ · DOI 10.1074/jbc.270.4.1721

    L-Arginine: transport, metabolic branches, nutrient interactions, availability and discovery questions (2026-09-18) · lines 70–76

    AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Rat cerebellar NOS preparation; separated partial reactions. · source_derived_draft · unverified_draft

    ## arg-nos-first Nitric-oxide production passes through a distinct intermediate. NOS converted arginine to N-hydroxyarginine in an oxygen- and calcium/calmodulin-dependent partial reaction. Model: Rat cerebellar NOS preparation; separated partial reactions. Limitations: Purified preparation; residual enzyme reductant supported a limited first reaction without added NADPH. This does not imply physiological NOS is NADPH independent. Evidence access: Primary abstract Characteristics of the nitric oxide synthase-catalyzed conversion of arginine to N-hydroxyarginine, the first oxygenation step in the enzymic synthesis of nitric oxide. · 1995 · https://pubmed.ncbi.nlm.nih.gov/7530247/ · DOI 10.1074/jbc.270.4.1721
    Complete structured claim and evidence

  3. The second oxygenation yielded NO and citrulline and required added NADPH and calcium/calmodulin.

    Nω-Hydroxy-L-arginine → NO source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Rat cerebellar NOS preparation; separated partial reactions.
    limitations
    Purified preparation; residual enzyme reductant supported a limited first reaction without added NADPH. This does not imply physiological NOS is NADPH independent.
    nutrient_topic
    L-Arginine collection; tissue, species, dose and formulation distinctions retained. · L-Arginine
    plain_language
    The next reaction produces the signal and recycles the carbon skeleton.
    primary_references
    Characteristics of the nitric oxide synthase-catalyzed conversion of arginine to N-hydroxyarginine, the first oxygenation step in the enzymic synthesis of nitric oxide. · 1995 · https://pubmed.ncbi.nlm.nih.gov/7530247/ · DOI 10.1074/jbc.270.4.1721

    L-Arginine: transport, metabolic branches, nutrient interactions, availability and discovery questions (2026-09-18) · lines 78–84

    AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Rat cerebellar NOS preparation; separated partial reactions. · source_derived_draft · unverified_draft

    ## arg-nos-second The next reaction produces the signal and recycles the carbon skeleton. The second oxygenation yielded NO and citrulline and required added NADPH and calcium/calmodulin. Model: Rat cerebellar NOS preparation; separated partial reactions. Limitations: Purified preparation; residual enzyme reductant supported a limited first reaction without added NADPH. This does not imply physiological NOS is NADPH independent. Evidence access: Primary abstract Characteristics of the nitric oxide synthase-catalyzed conversion of arginine to N-hydroxyarginine, the first oxygenation step in the enzymic synthesis of nitric oxide. · 1995 · https://pubmed.ncbi.nlm.nih.gov/7530247/ · DOI 10.1074/jbc.270.4.1721
    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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