ArticleeLife2016
Molecular mechanism of activation-triggered subunit exchange in Ca(2+)/calmodulin-dependent protein kinase II.
Article in eLife, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
67 citing papers in PubMed, 126 citations in OpenAlex.
- CaMKII as a Multimodal Signalling Hub in Neural Connectivity and Vulnerability.Molecular neurobiology · 2026Review
- Cx47 Phosphorylation Exacerbates White Matter Damage and Kainic Acid Induced Epilepsy.CNS neuroscience & therapeutics · 2025Article
- Nuclear CaMKII Isoforms as Regulators of Transcription: From Developmental to Pathological Persistence.Medical sciences (Basel, Switzerland) · 2025Review
- Degradation of CaMKII is stimulated by its active conformation.The Journal of biological chemistry · 2025Article
- A domain-swapped CaMKII conformation facilitates linker-mediated allosteric regulation.Nature communications · 2025Article
- An AlphaFold guided model for the evolution of the CaMKII interactome.bioRxiv : the preprint server for biology · 2025Article
- Exploring Large Protein Sequence Space through Homology- and Representation-based Hierarchical Clustering.Molecular biology and evolution · 2025Article
- Article
- Oxidation of CaMKIIα cysteines inhibits autonomous activation induced by phosphorylation.Archives of biochemistry and biophysics · 2025Article
- Sequential replacement of PSD95 subunits in postsynaptic supercomplexes is slowest in the cortex.eLife · 2024Article
- Ligand-induced CaMKIIα hub Trp403 flip, hub domain stacking, and modulation of kinase activity.Protein science : a publication of the Protein Society · 2024Article
- Hub stability in the calcium calmodulin-dependent protein kinase II.Communications biology · 2024Article
- Unveiling the role of CaMKII in retinal degeneration: from biological mechanism to therapeutic strategies.Cell & bioscience · 2024Review
- Ca2+/CaM dependent protein kinase II (CaMKII)α and CaMKIIβ hub domains adopt distinct oligomeric states and stabilities.Protein science : a publication of the Protein Society · 2024Article
- Role of CAMK2D in neurodevelopment and associated conditions.American journal of human genetics · 2024Article
- Methods optimization for the expression and purification of human calcium calmodulin-dependent protein kinase II alpha.PloS one · 2024Article
- Downregulated calmodulin expression contributes to endothelial cell impairment in diabetes.Acta pharmacologica Sinica · 2023Article
- Controlling the interaction between CaMKII and Calmodulin with a photocrosslinking unnatural amino acid.Protein science : a publication of the Protein Society · 2023Article
- Synaptic BMAL1 phosphorylation controls circadian hippocampal plasticity.Science advances · 2023Article
- Synaptic memory and CaMKII.Physiological reviews · 2023Review
7 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
15 authors at 4 institutions in 2 countries.
Funding
Abstract
Activation triggers the exchange of subunits in Ca(2+)/calmodulin-dependent protein kinase II (CaMKII), an oligomeric enzyme that is critical for learning, memory, and cardiac function. The mechanism by which subunit exchange occurs remains elusive. We show that the human CaMKII holoenzyme exists in dodecameric and tetradecameric forms, and that the calmodulin (CaM)-binding element of CaMKII can bind to the hub of the holoenzyme and destabilize it to release dimers. The structures of CaMKII from two distantly diverged organisms suggest that the CaM-binding element of activated CaMKII acts as a wedge by docking at intersubunit interfaces in the hub. This converts the hub into a spiral form that can release or gain CaMKII dimers. Our data reveal a three-way competition for the CaM-binding element, whereby phosphorylation biases it towards the hub interface, away from the kinase domain and calmodulin, thus unlocking the ability of activated CaMKII holoenzymes to exchange dimers with unactivated ones.
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What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.