ArticleCell reports2021
Conserved and divergent features of neuronal CaMKII holoenzyme structure, function, and high-order assembly.
Article in Cell reports, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 33 citations in OpenAlex.
- CaMKIIα holoenzymes self-organize into chain-like mesoscale clusters.Science advances · 2026Article
- CaMKIIβ insufficiency disrupts cortical networks, producing aberrant low-gamma oscillations and seizure susceptibility.Epilepsia · 2026Article
- CaMKII as a Multimodal Signalling Hub in Neural Connectivity and Vulnerability.Molecular neurobiology · 2026Review
- Structural dynamics of mixed-subunit CaMKIIα/β heterododecamers filmed by high-speed AFM.Nature communications · 2025Article
- A domain-swapped CaMKII conformation facilitates linker-mediated allosteric regulation.Nature communications · 2025Article
- Article
- A revised view of the role of CaMKII in learning and memory.Nature neuroscience · 2025Review
- Hub stability in the calcium calmodulin-dependent protein kinase II.Communications biology · 2024Article
- Studying CaMKII: Tools and standards.Cell reports · 2024Review
- The α-crystallin Chaperones Undergo a Quasi-ordered Co-aggregation Process in Response to Saturating Client Interaction.Journal of molecular biology · 2024Article
- 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
- Article
- N-Terminomic Changes in Neurons During Excitotoxicity Reveal Proteolytic Events Associated With Synaptic Dysfunctions and Potential Targets for Neuroprotection.Molecular & cellular proteomics : MCP · 2023Article
- Branch point strength controls species-specificLife science alliance · 2023Article
- CaMKIIα as a Promising Drug Target for Ischemic Grey Matter.Brain sciences · 2022Review
- Binary-FRET reveals transient excited-state structure associated with activity-dependent CaMKII - NR2B binding and adaptation.Nature communications · 2022Article
- Aβ-induced synaptic impairments require CaMKII activity that is stimulated by indirect signaling events.iScience · 2022Article
- Continuum dynamics and statistical correction of compositional heterogeneity in multivalent IDP oligomers resolved by single-particle EM.Journal of molecular biology · 2022Article
- Role of CaFrontiers in molecular neuroscience · 2022Review
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Neuronal CaMKII holoenzymes (α and β isoforms) enable molecular signal computation underlying learning and memory but also mediate excitotoxic neuronal death. Here, we provide a comparative analysis of these signaling devices, using single-particle electron microscopy (EM) in combination with biochemical and live-cell imaging studies. In the basal state, both isoforms assemble mainly as 12-mers (but also 14-mers and even 16-mers for the β isoform). CaMKIIα and β isoforms adopt an ensemble of extended activatable states (with average radius of 12.6 versus 16.8 nm, respectively), characterized by multiple transient intra- and inter-holoenzyme interactions associated with distinct functional properties. The extended state of CaMKIIβ allows direct resolution of intra-holoenzyme kinase domain dimers. These dimers could enable cooperative activation by calmodulin, which is observed for both isoforms. High-order CaMKII clustering mediated by inter-holoenzyme kinase domain dimerization is reduced for the β isoform for both basal and excitotoxicity-induced clusters, both in vitro and in neurons.
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