Cited by 328Neuroscience and Neuropharmacology ResearchProtein Kinase Regulation and GTPase SignalingGenetics and Neurodevelopmental Disorders

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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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Okamoto, Ken-Ichi, Narayanan, Radhakrishnan, Lee, Sang H., Murata, Kazuyoshi, Hayashi, Yasunori·2007·Proceedings of the National Academy of Sciences

DOI 10.1073/pnas.0701656104PMC PMC1851051

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Abstract

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 CaMKII b dissociates from F-actin because of competition with Ca 2 1 / CaM for the F-actin binding region, and dissociation is made more persistent by speci ﬁ c autophosphorylation of CaMKII b in the F-actin binding region (171 – 174).”
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Self-citation
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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
ORCID: Lee, Sang H.
Murata, Kazuyoshi
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
DOI: 10.1073/pnas.0701656104
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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The role of CaMKII as an F-actin-bundling protein crucial for maintenance of dendritic spine structure

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