Component

Ca2+/calmodulin-dependent protein kinase II family

Independent biological entity. Read linked claims for experimental scope and context.

6 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. Partial autophosphorylation generates CaMKII activity that persists in the absence of calcium in the purified assay.

    Ca2+/calmodulin-dependent protein kinase II family → Autophosphorylated CaMKII with autonomous activity 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
    Autonomy depends on phosphorylation conditions; not all self-phosphorylation activates and persistence in living cells is not quantified.
    nutrient_topic
    Calcium research collection; topical membership is not evidence of a direct dietary effect. · Calcium
    organism
    Mammalia
    plain_language
    After activation, CaMKII can retain activity beyond the calcium pulse.
    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
    protein_modification
    tissue_or_cell_type
    Brain enzyme preparation

    Calcium: mechanism-first literature curation (2026-09-17) · lines 451–462

    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-autonomous-activity Partial autophosphorylation generates CaMKII activity that persists in the absence of calcium in the purified assay. Condition category: normal nutrient_topic: Calcium research collection; topical membership is not evidence of a direct dietary effect. plain_language: After activation, CaMKII can retain activity beyond the calcium pulse. organism: Mammalia tissue_or_cell_type: Brain enzyme preparation experimental_model: Purified mammalian brain CaMKII; phosphorylation and substrate-kinase assays limitations: Autonomy depends on phosphorylation conditions; not all self-phosphorylation activates and persistence in living cells is not quantified. research_relationship_category: protein_modification 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

What acts on it

  1. 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

  2. Rabbit hearts exposed to 2.7 mM K showed increased CaMKII activity; KN-93 prevented low-K early afterdepolarizations and ventricular arrhythmia.

    Extracellular potassium concentration → Ca2+/calmodulin-dependent protein kinase II family source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    nutrient_deficiency Imported condition classification; unverified.
    cross_nutrient
    Potassium depletion of the bath alters calcium-dependent signaling.
    experimental_model
    Isolated hearts; enzyme assay and inhibitor intervention.
    limitations
    Pharmacology is not genetic specificity; clinical efficacy was not tested.
    nutrient_topic
    Potassium research collection; topical membership is not evidence of a direct dietary effect. · Potassium
    organism
    Rabbit and rat experimental series
    plain_language
    Calcium-sensitive kinase signaling contributed to electrical instability.
    primary_references
    [pezhouman-2015-camkii] Molecular Basis of Hypokalemia-Induced Ventricular Fibrillation (2015). https://pubmed.ncbi.nlm.nih.gov/26269574/ DOI: 10.1161/CIRCULATIONAHA.115.016217
    tissue_or_cell_type
    Ventricular myocardium
    trigger_kind
    nutrient_deficiency Imported condition classification; unverified.

    Potassium: cross-nutrient mechanisms and deficiency (2026-09-17) · lines 645–655

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Isolated hearts; enzyme assay and inhibitor intervention. · source_derived_draft · unverified_draft

    ### k-low-activates-camkii Rabbit hearts exposed to 2.7 mM K showed increased CaMKII activity; KN-93 prevented low-K early afterdepolarizations and ventricular arrhythmia. Condition category: nutrient_deficiency nutrient_topic: Potassium research collection; topical membership is not evidence of a direct dietary effect. plain_language: Calcium-sensitive kinase signaling contributed to electrical instability. organism: Rabbit and rat experimental series tissue_or_cell_type: Ventricular myocardium experimental_model: Isolated hearts; enzyme assay and inhibitor intervention. limitations: Pharmacology is not genetic specificity; clinical efficacy was not tested. cross_nutrient: Potassium depletion of the bath alters calcium-dependent signaling. [pezhouman-2015-camkii] Molecular Basis of Hypokalemia-Induced Ventricular Fibrillation (2015). https://pubmed.ncbi.nlm.nih.gov/26269574/ DOI: 10.1161/CIRCULATIONAHA.115.016217
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. Oxidation of paired CaMKII regulatory methionines sustained kinase activity after calcium/calmodulin was removed.

    Protein-bound methionine → Oxidized regulatory methionines in the CaMKII study source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Biochemical kinase assays with cardiomyocyte and mouse experiments; exact purified construct species not resolved here.
    limitations
    Initial calcium/calmodulin exposure and sustained autonomous activity are distinct; not a dietary methionine effect.
    nutrient_topic
    L-Methionine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Methionine
    plain_language
    Oxidation can leave a signaling protein switched on.
    primary_references
    A dynamic pathway for calcium-independent activation of CaMKII by methionine oxidation. · 2008 · https://pubmed.ncbi.nlm.nih.gov/18455987/ · DOI 10.1016/j.cell.2008.02.048

    L-Methionine: transport, methylation, sulfur metabolism and cross-nutrient mechanisms (2026-09-19) · lines 332–338

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Biochemical kinase assays with cardiomyocyte and mouse experiments; exact purified construct species not resolved here. · source_derived_draft · unverified_draft

    ## methionine-camkii-oxidation Oxidation can leave a signaling protein switched on. Oxidation of paired CaMKII regulatory methionines sustained kinase activity after calcium/calmodulin was removed. Model: Biochemical kinase assays with cardiomyocyte and mouse experiments; exact purified construct species not resolved here. Limitations: Initial calcium/calmodulin exposure and sustained autonomous activity are distinct; not a dietary methionine effect. Evidence access: Primary abstract A dynamic pathway for calcium-independent activation of CaMKII by methionine oxidation. · 2008 · https://pubmed.ncbi.nlm.nih.gov/18455987/ · DOI 10.1016/j.cell.2008.02.048
    Complete structured claim and evidence

  2. Msra-null mice had greater CaMKII oxidation, myocardial apoptosis and post-infarction dysfunction; methionine-sulfoxide reduction reversed oxidation-dependent activation in supporting assays.

    Mouse methionine sulfoxide reductase A / Msra → Oxidized CaMKII and cardiac injury in mice source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    evidence_access
    Primary abstract
    experimental_model
    Msra-knockout mice with biochemical support.
    limitations
    MSRA and selenium-dependent MSRB1 differ in substrate stereochemistry; they are not interchangeable.
    nutrient_topic
    L-Methionine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Methionine
    plain_language
    Repairing an oxidized residue can reset a signaling switch.
    primary_references
    A dynamic pathway for calcium-independent activation of CaMKII by methionine oxidation. · 2008 · https://pubmed.ncbi.nlm.nih.gov/18455987/ · DOI 10.1016/j.cell.2008.02.048
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    L-Methionine: transport, methylation, sulfur metabolism and cross-nutrient mechanisms (2026-09-19) · lines 340–346

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Msra-knockout mice with biochemical support. · source_derived_draft · unverified_draft

    ## methionine-msra-camkii-repair Repairing an oxidized residue can reset a signaling switch. Msra-null mice had greater CaMKII oxidation, myocardial apoptosis and post-infarction dysfunction; methionine-sulfoxide reduction reversed oxidation-dependent activation in supporting assays. Model: Msra-knockout mice with biochemical support. Limitations: MSRA and selenium-dependent MSRB1 differ in substrate stereochemistry; they are not interchangeable. Evidence access: Primary abstract A dynamic pathway for calcium-independent activation of CaMKII by methionine oxidation. · 2008 · https://pubmed.ncbi.nlm.nih.gov/18455987/ · DOI 10.1016/j.cell.2008.02.048
    Complete structured claim and evidence

  3. GS-967 suppressed hypokalemic early afterdepolarizations; simulations implicated CaMKII-enhanced late sodium current in a sodium/calcium feedback loop.

    Cardiac late sodium current → Cardiac early afterdepolarizations source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    nutrient_deficiency Imported condition classification; unverified.
    cross_nutrient
    Sodium entry and calcium loading interact during low extracellular potassium.
    experimental_model
    Low-K cardiac inhibition experiments and computational model.
    limitations
    The complete feedback sequence is model-supported, not every step directly measured.
    nutrient_topic
    Potassium research collection; topical membership is not evidence of a direct dietary effect. · Potassium
    organism
    Rabbit/rat and mathematical model
    plain_language
    Persistent sodium entry helped sustain low-potassium electrical instability.
    primary_references
    [pezhouman-2015-camkii] Molecular Basis of Hypokalemia-Induced Ventricular Fibrillation (2015). https://pubmed.ncbi.nlm.nih.gov/26269574/ DOI: 10.1161/CIRCULATIONAHA.115.016217
    tissue_or_cell_type
    Ventricular myocardium
    trigger_kind
    nutrient_deficiency Imported condition classification; unverified.

    Potassium: cross-nutrient mechanisms and deficiency (2026-09-17) · lines 657–667

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Low-K cardiac inhibition experiments and computational model. · source_derived_draft · unverified_draft

    ### k-low-late-sodium-feedback GS-967 suppressed hypokalemic early afterdepolarizations; simulations implicated CaMKII-enhanced late sodium current in a sodium/calcium feedback loop. Condition category: nutrient_deficiency nutrient_topic: Potassium research collection; topical membership is not evidence of a direct dietary effect. plain_language: Persistent sodium entry helped sustain low-potassium electrical instability. organism: Rabbit/rat and mathematical model tissue_or_cell_type: Ventricular myocardium experimental_model: Low-K cardiac inhibition experiments and computational model. limitations: The complete feedback sequence is model-supported, not every step directly measured. cross_nutrient: Sodium entry and calcium loading interact during low extracellular potassium. [pezhouman-2015-camkii] Molecular Basis of Hypokalemia-Induced Ventricular Fibrillation (2015). https://pubmed.ncbi.nlm.nih.gov/26269574/ DOI: 10.1161/CIRCULATIONAHA.115.016217
    Complete structured claim and evidence

In the sources

Preserved passages that mention this component, quoted exactly. Open one to read it in context.

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