ArticleBiophysical journal2015
Covert Changes in CaMKII Holoenzyme Structure Identified for Activation and Subsequent Interactions.
Article in Biophysical journal, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 22 citations in OpenAlex.
- CaMKIIα holoenzymes self-organize into chain-like mesoscale clusters.Science advances · 2026Article
- Structural dynamics of mixed-subunit CaMKIIα/β heterododecamers filmed by high-speed AFM.Nature communications · 2025Article
- Fluorescence Lifetime Imaging Techniques-A Review on Principles, Applications and Clinical Relevance.Journal of biophotonics · 2025Review
- Hub stability in the calcium calmodulin-dependent protein kinase II.Communications biology · 2024Article
- Real-time single-molecule imaging of CaMKII-calmodulin interactions.Biophysical journal · 2024Article
- Binary-FRET reveals transient excited-state structure associated with activity-dependent CaMKII - NR2B binding and adaptation.Nature communications · 2022Article
- Conformational spread drives the evolution of the calcium-calmodulin protein kinase II.Scientific reports · 2022Article
- Conserved and divergent features of neuronal CaMKII holoenzyme structure, function, and high-order assembly.Cell reports · 2021Article
- A Guide to Fluorescence Lifetime Microscopy and Förster's Resonance Energy Transfer in Neuroscience.Current protocols in neuroscience · 2020Review
- Structural Insights into the Regulation of CaCold Spring Harbor perspectives in biology · 2020Review
- VenusBiophysical journal · 2019Article
- Conformational coupling by trans-phosphorylation in calcium calmodulin dependent kinase II.PLoS computational biology · 2019Article
- The CaMKII/NMDA receptor complex controls hippocampal synaptic transmission by kinase-dependent and independent mechanisms.Nature communications · 2018Article
- Auto-FPFA: An Automated Microscope for Characterizing Genetically Encoded Biosensors.Scientific reports · 2018Article
- Deciphering CaMKII Multimerization Using Fluorescence Correlation Spectroscopy and Homo-FRET Analysis.Biophysical journal · 2017Article
- Zinc-Induced Polymerization of Killer-Cell Ig-like Receptor into Filaments Promotes Its Inhibitory Function at Cytotoxic Immunological Synapses.Molecular cell · 2016Article
- Review
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Between 8 to 14 calcium-calmodulin (Ca(2+)/CaM) dependent protein kinase-II (CaMKII) subunits form a complex that modulates synaptic activity. In living cells, the autoinhibited holoenzyme is organized as catalytic-domain pairs distributed around a central oligomerization-domain core. The functional significance of catalytic-domain pairing is not known. In a provocative model, catalytic-domain pairing was hypothesized to prevent ATP access to catalytic sites. If correct, kinase-activity would require catalytic-domain pair separation. Simultaneous homo-FRET and fluorescence correlation spectroscopy was used to detect structural changes correlated with kinase activation under physiological conditions. Saturating Ca(2+)/CaM triggered Threonine-286 autophosphorylation and a large increase in CaMKII holoenzyme hydrodynamic volume without any appreciable change in catalytic-domain pair proximity or subunit stoichiometry. An alternative hypothesis is that two appropriately positioned Threonine-286 interaction-sites (T-sites), each located on the catalytic-domain of a pair, are required for holoenzyme interactions with target proteins. Addition of a T-site ligand, in the presence of Ca(2+)/CaM, elicited a large decrease in catalytic-domain homo-FRET, which was blocked by mutating the T-site (I205K). Apparently catalytic-domain pairing is altered to allow T-site interactions.
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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.