The DOI matches its Crossref record; 37 of the 38 references it cites were found in a registry or an index.
The role of CaMKII as an F-actin-bundling protein crucial for maintenance of dendritic spine structure
Open accessAbstract
Ca 2+ -calmodulin-dependent protein kinase II (CaMKII) is a serine/threonine protein kinase critically involved in synaptic plasticity in the brain. It is highly concentrated in the postsynaptic density fraction, exceeding the amount of any other signal transduction molecules. Because kinase signaling can be amplified by catalytic reaction, why CaMKII exists in such a large quantity has been a mystery. Here, we provide biochemical evidence that CaMKII is capable of bundling F-actin through a stoichiometric interaction. Consistent with this evidence, in hippocampal neurons, RNAi-mediated down-regulation of CaMKII leads to a reduction in the volume of dendritic spine head that is mediated by F-actin dynamics. An overexpression of CaMKII slowed down the actin turnover in the spine head. This activity was associated with β subunit of CaMKII in a manner requiring its actin-binding and association domains but not the kinase domain. This finding indicates that CaMKII serves as a central signaling molecule in both functional and structural changes during synaptic plasticity.
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“Upon activation CaMKIIβ dissociates from F-actin because of competition with Ca2+/CaM for the F-actin binding region, and dissociation is made more persistent by specific autophosphorylation of CaMKIIβ in the F-actin binding region (171–174).”
From Synaptic memory and CaMKII (2023) · cites this paper as [174]
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“CaMKII is a calcium-activated kinase involved in structural plasticity by remodeling of the postsynaptic density (Yoshimura et al., 2002), rearrangement of the actin cytoskeleton (Okamoto et al., 2007) and maintenance of spine enlargement (Matsuzaki et al., 2004; Lee et al., 2009).”
From Barriers in the brain: resolving dendritic spine morphology and compartmentalization (2014) · cites this paper as Okamoto et al., 2007
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Cites
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Self-citationMorphological Changes in Dendritic Spines Associated with Long-Term Synaptic Plasticity
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Liang, J., Sood, A., Khanna, G., & Rankin, C. H. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.06.26.661804
Actin's role in signaling light-induced phase shifts in the mammalian circadian clock
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Kim, S. M. (2007) · UA Campus Repository (The University of Arizona)
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Mondal, R., Banerjee, C., Nandy, S., Roy, M., & Chakraborty, J. (2023) · Figshare · doi:10.6084/m9.figshare.23819964
Mondal, R., Banerjee, C., Nandy, S., Roy, M., & Chakraborty, J. (2023) · Figshare · doi:10.6084/m9.figshare.23819982
Mondal, R., Banerjee, C., Nandy, S., Roy, M., & Chakraborty, J. (2023) · Figshare · doi:10.6084/m9.figshare.23819976
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Formation, stability, and competition in dendritic proto-spinesPreprint
Pulikkottil, V. V., & Bhalla, U. S. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.01.09.697842
CaMKIIα holoenzymes self-organize into worm-like mesoscale clustersPreprint
Suzuki, T., Sumikama, T., Matsushima, K., Hasegawa, K., Sumino, A., Umeda, K., Kodera, N., Das, T., Beta, C., Murakoshi, H., et al. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.01.21.700754
The Role of Actin Depolymerization in the Mechanisms of Long-Term Potentiation
Kudryashova, I. V. (2026) · Neuroscience and Behavioral Physiology · doi:10.1007/s11055-026-01958-5
The Scrib1 Interactome and its relevance for synaptic plasticity & neurodevelopmental disorders
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Noncoding RNAs regulating serine/threonine kinases in neurodegeneration
Khamineh, Y., Ghiasvand, M., Zolghadri, S., & Saboury, A. A. (2026) · Elsevier eBooks · doi:10.1016/b978-0-443-44173-8.00007-3
CaMKII–LUZP1 signaling couples cytoskeletal acetylation and autophagy to drive neuronal plasticityPreprint
Tsai, C., Kuroda, K., Oka, Y., Taniguchi, M., Yagi, H., & Sato, M. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.07.03.736264
The how and why for multiple forms of hippocampal LTP
Gall, C. M., Le, A. A., & LYNCH, G. S. (2026) · Frontiers in Synaptic Neuroscience · doi:10.3389/fnsyn.2026.1855059
Vargas-Hernández, S., bueno, C., Syeda, M., Pham, J., Mireles, L. L., Mauro, C. M. D., Wolynes, P. G., Waxham, M. N., & Gustavsson, A. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.09.16.752118
Metadata
- Authors
- Okamoto, K.-I., Narayanan, R., Lee, S. H., Murata, K., & Hayashi, Y.
- Affiliations
- *RIKEN-MIT Neuroscience Research Center, The Picower Institute for Learning and Memory, Department of Brain and Cognitive Sciences, Massachusetts Institute of Technology, Cambridge, MA 02139;
- Massachusetts Institute of Technology (US)
- Medical College of Wisconsin (US)
- Corresponding author
- Hayashi, Yasunori
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2007-04-10
- Volume
- 104
- Issue
- 15
- Pages
- 6418-6423
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC1851051
- OpenAlex
- W2170201765
- Cited by
- 328
- References
- 38
- Citations by year
- 2026: 13 · 2025: 14 · 2024: 12 · 2023: 20 · 2022: 10 · 2021: 13 · 2020: 14 · 2019: 18 · 2018: 20 · 2017: 16 · 2016: 14 · 2015: 19 · 2014: 29 · 2013: 17 · 2012: 20
- FWCI
- 8.49
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Ellison Medical Foundation
- National Institutes of Health
- RIKEN
- National Institute on Drug Abuse (R01DA017310)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Genetics and Neurodevelopmental Disorders
- Keywords
- CaMKII, F-actin bundling, synaptic plasticity, postsynaptic density, actin turnover, beta subunit, actin-binding domain, hippocampal neurons
- MeSH terms
- Actins, Animals, Hippocampus, Microscopy, Electron, Scanning, Models, Biological, Neuronal Plasticity, Synapses, Signal Transduction, Calcium-Calmodulin-Dependent Protein Kinases, RNA Interference, Dendritic Spines, Rats, Calcium-Calmodulin-Dependent Protein Kinase Type 2
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