The impacts of geometry and binding on CaMKII diffusion and retention in dendritic spines
Open accessAbstract
We used a particle-based Monte Carlo simulation to dissect the regulatory mechanism of molecular translocation of CaMKII, a key regulator of neuronal synaptic function. Geometry was based upon measurements from EM reconstructions of dendrites in CA1 hippocampal pyramidal neurons. Three types of simulations were performed to investigate the effects of geometry and other mechanisms that control CaMKII translocation in and out of dendritic spines. First, the diffusional escape rate of CaMKII from model spines of varied morphologies was examined. Second, a postsynaptic density (PSD) was added to study the impact of binding sites on this escape rate. Third, translocation of CaMKII from dendrites and trapping in spines was investigated using a simulated dendrite. Based on diffusion alone, a spine of average dimensions had the ability to retain CaMKII for duration of ~4 s. However, binding sites mimicking those in the PSD controlled the residence time of CaMKII in a highly nonlinear manner. In addition, we observed that F-actin at the spine head/neck junction had a significant impact on CaMKII trapping in dendritic spines. We discuss these results in the context of possible mechanisms that may explain the experimental results that have shown extended accumulation of CaMKII in dendritic spines during synaptic plasticity and LTP induction.
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Additional modeling studies have shown that the effective CaMKII diffusion constant depends heavily on binding to synaptic scaffolds and the actin cytoskeleton in spine necks.
“and additional modeling studies have shown that the effective CaMKII diffusion constant depends heavily on binding to synaptic scaffolds and the actin cytoskeleton in spine necks (Byrne et al., 2011).”
From Barriers in the brain: resolving dendritic spine morphology and compartmentalization (2014) · cites this paper as Byrne et al., 2011
The Results (§3.4–3.5; page not available) model CaMKII binding to targets in the postsynaptic density and show that F-actin spacing at the spine neck–head boundary can strongly restrict diffusion. The claim overstates the mechanism: the paper models F-actin as a physical barrier, not binding to actin in the neck, and reports effects on escape and retention rather than a binding-dependent effective diffusion constant. (LLM, conf=0.88)
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Self-citation
- Authors
- Byrne, M. J., Waxham, M. N., & Kubota, Y.
- Corresponding author
- Kubota, Yoshihisa
- ORCID
- Waxham, M. Neal
- Venue
- Journal of Computational Neuroscience
- Published
- 2010-11-23
- Volume
- 31
- Issue
- 1
- Pages
- 1-12
- ISSN
- 0929-5313 (ISSN-L)
- 1573-6873
- PMC
- PMC3617044
- OpenAlex
- W2032123789
- Cited by
- 41
- References
- 40
- Citations by year
- 2026: 1 · 2025: 1 · 2023: 1 · 2022: 3 · 2021: 3 · 2020: 4 · 2019: 7 · 2017: 2 · 2016: 2 · 2014: 5 · 2013: 3 · 2012: 6
- FWCI
- 1.55
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Journal of Computational Neuroscience (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institutes of Health (5p01ns038310-10)
- National Institute of Neurological Disorders and Stroke (P01 NS-038310, NS038310)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Life Sciences › Neuroscience › Cognitive Neuroscience › Neural dynamics and brain function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Keywords
- CaMKII, dendritic spines, protein diffusion, postsynaptic density, binding sites, spine geometry, F-actin, synaptic plasticity, long-term potentiation, CA1 pyramidal neurons, protein retention, Monte Carlo simulation
- MeSH terms
- Computer Simulation, Diffusion, Hippocampus, Humans, Models, Neurological, Monte Carlo Method, Neurons, Dendritic Spines, Calcium-Calmodulin-Dependent Protein Kinase Type 2
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