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The role of CaMKII as an F-actin-bundling protein crucial for maintenance of dendritic spine structure
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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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A synaptic model of memory: long-term potentiation in the hippocampus
Bliss, T. V. P., & Collingridge, G. L. (1993) · Nature · doi:10.1038/361031a0 · Cited by 11,566
A Multiple Comparison Procedure for Comparing Several Treatments with a Control
Dunnett, C. W. (1955) · Journal of the American Statistical Association · doi:10.1080/01621459.1955.10501294 · Cited by 6,097
AMPA Receptor Trafficking and Synaptic Plasticity
Malinow, R., & Malenka, R. C. (2002) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.25.112701.142758 · Cited by 2,588
Structural basis of long-term potentiation in single dendritic spines
Matsuzaki, M., Honkura, N., Ellis-Davies, G. C. R., & Kasai, H. (2004) · Nature · doi:10.1038/nature02617 · Cited by 2,483
The molecular basis of CaMKII function in synaptic and behavioural memory
Lisman, J., Schulman, H., & Cline, H. (2002) · Nature Reviews Neuroscience · doi:10.1038/nrn753 · Cited by 1,860
Hayashi, Y., Shi, S.-H., Esteban, J. A., Piccini, A., Poncer, J.-C., & Malinow, R. (2000) · Science · doi:10.1126/science.287.5461.2262 · Cited by 1,524
Self-citationRapid Spine Delivery and Redistribution of AMPA Receptors After Synaptic NMDA Receptor Activation
Shi, S.-H., Hayashi, Y., Petralia, R. S., Zaman, S. H., Wenthold, R. J., Svoboda, K., & Malinow, R. (1999) · Science · doi:10.1126/science.284.5421.1811 · Cited by 1,276
Self-citationMorphological Changes in Dendritic Spines Associated with Long-Term Synaptic Plasticity
Yuste, R., & Bonhoeffer, T. (2001) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.24.1.1071 · Cited by 1,269
Regulatory phosphorylation of AMPA-type glutamate receptors by CaM-KII during long-term potentiation
Barria, A., Muller, D., Derkach, V., Griffith, L. C., & Soderling, T. R. (1997) · Science · doi:10.1126/science.276.5321.2042 · Cited by 1,049
Structural plasticity and memory
Lamprecht, R., & LeDoux, J. (2004) · Nature Reviews Neuroscience · doi:10.1038/nrn1301 · Cited by 1,010
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Zhai, J., Navakkode, S., Yeow, S. Q. Z., Krishna-K, K., Liang, M. C., Koh, J. H., Wong, R. X., Yu, W., Sajikumar, S., Huang, H. Y., et al. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2203883119 · Cited by 12
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Chuah, Y. H., Tay, E. X. Y., Grinchuk, O. V., Yoon, J., Feng, J., Kannan, S., Robert, M., Jakhar, R., Liang, Y., Lee, B. W. L., et al. (2023) · Cell Death and Differentiation · doi:10.1038/s41418-023-01192-3 · Cited by 11
The Function of CaM Kinase II in Synaptic Plasticity and Spine Formation
Fukunaga, K., Shioda, N., & Miyamoto, E. (2009) · Springer eBooks · doi:10.1007/978-0-387-30370-3_9 · Cited by 12
CaMKIIβ knockdown decreases store-operated calcium entry in hippocampal dendritic spines
Zernov, N., Борисович, Б. И., & Александровна, П. Е. (2022) · IBRO Neuroscience Reports · doi:10.1016/j.ibneur.2022.01.001 · Cited by 12
A Uniform and Isotropic Cytoskeletal Tiling Fills Dendritic Spines
Eberhardt, F., Bushong, E. A., Phan, S., Peltier, S. T., Monteagudo-Mesas, P., Weinkauf, T., Herz, A. V. M., Stemmler, M., & Ellisman, M. H. (2022) · eNeuro · doi:10.1523/eneuro.0342-22.2022 · Cited by 12
NMDA receptors on zebrafish M authner cells require CaMKII‐α for normal development
Roy, B., Ferdous, J., & Ali, D. W. (2014) · Developmental Neurobiology · doi:10.1002/dneu.22214 · Cited by 11
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Liu, Y., & Templeton, D. M. (2012) · Journal of Cellular Physiology · doi:10.1002/jcp.24108 · Cited by 12
Zhang, Z., Zhou, W., Fan, J., Ren, Y., & Yin, G. (2013) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2013.01.006 · Cited by 12
Developmental restoration of LTP deficits in heterozygous CaMKIIα KO mice
Goodell, D. J., Benke, T. A., & Bayer, K. U. (2016) · Journal of Neurophysiology · doi:10.1152/jn.00518.2016 · Cited by 12
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Kretzschmar, A., Schülke, J.-P., Masana, M., Dürre, K., Müller, M. B., Bausch, A. R., & Rein, T. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19123993 · Cited by 12
Insights from graph theory on the morphologies of actomyosin networks with multilinkers
Eliaz, Y., Nédélec, F., Morrison, G., Levine, H., & Cheung, M. S. (2020) · Physical review. E · doi:10.1103/physreve.102.062420 · Cited by 12
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Yuan, Y., & Ferguson, L. R. (2011) · Lifestyle Genomics · doi:10.1159/000327902 · Cited by 11
Yin, P., Xu, H., Wang, Q., Wang, J., Yin, L., Xu, M., Xie, Z., Liu, W., & Cao, X. (2016) · Neuropharmacology · doi:10.1016/j.neuropharm.2016.12.013 · Cited by 10
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Hyde, D. R., & Lahne, M. (2017) · Neural Regeneration Research · doi:10.4103/1673-5374.213533 · Cited by 10
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Kim, K., Suzuki, A., Kojima, H., Kawamura, M., Miya, K., Abe, M., Yamada, I., Furuse, T., Wakana, S., Sakimura, K., et al. (2018) · Neurobiology of Learning and Memory · doi:10.1016/j.nlm.2018.12.003 · Cited by 11
Self-citationSaneyoshi, T. (2021) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2021.01.018 · Cited by 9
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Liu, X., Li, S., Zhang, W., Xie, Z., He, J., Zhang, X., Yu, S., Cao, S., Yu, T., & Xiao, Z. (2022) · iScience · doi:10.1016/j.isci.2022.104989 · Cited by 9
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Yang, C., Zhang, M., Li, S., Yi, F., Huang, H., Xie, H., Liu, H., Huang, R., & Zhou, J. (2022) · Neuroscience · doi:10.1016/j.neuroscience.2022.08.019 · Cited by 9
Liu, J., Zhou, R., He, Q., Li, W.-I., Zhang, T., Niu, B., Zheng, X., & Xie, J. (2009) · NeuroToxicology · doi:10.1016/j.neuro.2009.03.006 · Cited by 9
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Feng, T., Xu, Q., Wang, S., Hou, D., & Wu, X. (2025) · Biochemistry and Biophysics Reports · doi:10.1016/j.bbrep.2025.102065 · Cited by 8
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CaMKII: the Swiss army knife of synaptic plasticity
Kim, K., & Hayashi, Y. (2014) · The Journal of Physiology · doi:10.1113/jphysiol.2014.284414 · Cited by 6
Self-citationWang, Y., Troughton, L. D., Xu, F., Chatterjee, A., Ding, C., Zhao, H., Cifuentes, L. P., Wagner, R., Wang, T., Tan, S., et al. (2023) · eLife · doi:10.7554/elife.88828 · Cited by 5
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Neely, M. D., Robert, E. M., Baucum, A. J., Colbran, R. J., Muly, E. C., & Deutch, A. Y. (2009) · Brain Research · doi:10.1016/j.brainres.2009.03.067 · Cited by 5
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Abouelezz, A. M., Minkeviciene, R., & Hotulainen, P. (2016) · Springer eBooks · doi:10.1007/978-4-431-56050-0_2 · Cited by 4
Inoue, R., Nishi, H., Osaka, M., Yoshida, M., & Nangaku, M. (2022) · The Journal of Immunology · doi:10.4049/jimmunol.2001349 · Cited by 4
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Kudryashova, I. V. (2019) · Neurochemical Journal · doi:10.1134/s1819712419010136 · Cited by 4
Zheng, J., Redmond, L., Xu, C., Kuang, J., & Liao, W. (2014) · PubMed Central · Cited by 4
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Cervia, D. (2011) · General Physiology and Biophysics · doi:10.4149/gpb_2011_03_251 · Cited by 3
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Urbano, F. J., Bisagno, V., & García‐Rill, E. (2019) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00374.2019 · Cited by 3
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Strack, S., & Hell, J. W. (2008) · Springer eBooks · doi:10.1007/978-0-387-77232-5_16 · Cited by 3
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Rangamani, P., Levy, M., Khan, S., & OSTER, G. F. (2016) · Biophysical Journal · doi:10.1016/j.bpj.2015.11.2003 · Cited by 3
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House, S. J., Zachar, M. M., Ginnan, R. G., Riper, D. A. V., & Singer, H. A. (2008) · Springer eBooks · doi:10.1007/978-0-387-09552-3_18 · Cited by 3
Cooper, D. B. (2011) · Mental Health and Substance Use · doi:10.1080/17523281.2011.533433 · Cited by 3
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Deguchi, A., Hata, M., Uhara, T., & Yamauchi, T. (2008) · Brain Research · doi:10.1016/j.brainres.2008.07.070 · Cited by 1
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Okuno, H., Araki, A., & Minatohara, K. (2015) · Springer eBooks · doi:10.1007/978-3-319-24364-1_6 · Cited by 1
Nichols, T. W. (2023) · Journal of Multiscale Neuroscience · doi:10.56280/1564010613 · Cited by 2
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Novak, G. (2008) · TSpace (University of Toronto) · Cited by 1
Luyben, T. T. (2018) · TSpace (University of Toronto) · Cited by 1
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Valencia, M. (2018) · TSpace (University of Toronto) · Cited by 1
Negri, F., Luboeinski, J., Tetzlaff, C., & Fauth, M. J. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.02.18.638822 · Cited by 1
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Redondo, R. L., & Morris, R. (2014) · Springer eBooks · doi:10.1007/978-1-4939-1761-7_1
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Midgley, A. C. (2014) · ORCA Online Research @Cardiff (Cardiff University)
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Hanamura, K., & Shirao, T. (2007) · Folia Pharmacologica Japonica · doi:10.1254/fpj.130.352
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Bragg (2020) · Western CEDAR (Western Washington University) · doi:10.25710/yzvc-bd79
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Brown, C. A. (2015) · YorkSpace (York University)
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Schenk, G. J. (2010) · Leiden Repository (Leiden University)
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Podor, B. (2017) · DalSpace (Dalhousie University)
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Li, Q. (2015) · Digitale Bibliothek Braunschweig (Verbundzentrale Göttingen (VZG)) · doi:10.24355/dbbs.084-201503260942-0
Oliver, & Robert, J. (2017) · UNM’s Digital Repository (University of New Mexico)
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Khan, S., Molloy, J., & Downing, K. (2018) · bioRxiv · doi:10.1101/308353
Labrecque, S. (2012) · Corpus Université Laval (Université Laval)
Ramachandran, P. (2009) · The Journal of the American Medical Association (JAMA) Network (American Medical Association) · doi:10.13028/e8pg-tq46
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Borovac, J. (2019) · TSpace (University of Toronto)
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Tone, D., Ode, K. L., Zhang, Q., Fujishima, H., Yamada, R. G., Nagashima, Y., Matsumoto, K., Wen, Z., Yoshida, S. Y., Mitani, T. T., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.10.11.463945
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Wolynski, J. J. (2014) · viXra
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Silbern, I. (2021) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-8895
Hell, J. W. (2010) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.5047958.4982062
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Lin, W., & Webb, D. J. (2014) · The Open Neuroscience Journal · doi:10.2174/1874082000903010054
Bolton, S. C., Thompson, D. H., & Kinzer‐Ursem, T. L. (2024) · PLoS ONE · doi:10.1371/journal.pone.0285651
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Bayer, K. U., Brown, C. N., & Giese, K.-P. (2024) · Elsevier eBooks · doi:10.1016/b978-0-443-15754-7.00057-2
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Hur, M., Bartol, T. M., Rangamani, P., B, T. J. S. A., & Mjolsness, E. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.04.18.649558
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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