A Temporary Gating of Actin Remodeling during Synaptic Plasticity Consists of the Interplay between the Kinase and Structural Functions of CaMKII
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The structural modification of dendritic spines plays a critical role in synaptic plasticity. CaMKII is a pivotal molecule involved in this process through both kinase-dependent and independent structural functions, but the respective contributions of these two functions to the synaptic plasticity remain unclear. We demonstrate that the transient interplay between the kinase and structural functions of CaMKII during the induction of synaptic plasticity temporally gates the activity-dependent modification of the actin cytoskeleton. Inactive CaMKII binds F-actin, thereby limiting access of actin-regulating proteins to F-actin and stabilizing spine structure. CaMKII-activating stimuli trigger dissociation of CaMKII from F-actin through specific autophosphorylation reactions within the F-actin binding region and permits F-actin remodeling by regulatory proteins followed by reassociation and restabilization. Blocking the autophosphorylation impairs both functional and structural plasticity without affecting kinase activity. These results underpin the importance of the interplay between the kinase and structural functions of CaMKII in defining a time window permissive for synaptic plasticity.
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The defect caused by CaMKIIβ deletion cannot be rescued by a mutant form of CaMKIIβ that cannot bind to F-actin.
“The defect caused by CaMKIIβ deletion cannot be rescued by a mutant form of CaMKIIβ that cannot bind to F-actin (172).”
From Synaptic memory and CaMKII (2023) · cites this paper as [172]
In Results, “Dissociation of CaMKIIβ from F-actin is necessary for functional and structural LTP” (page not available), the paper reports that the All A mutant failed to rescue the LTP reduction caused by CaMKIIβ shRNA. But All A retains F-actin binding; the binding-deficient All D mutant is described in Results, “Autophosphorylation sites on the F-actin binding region of CaMKIIβ regulate interaction with F-actin” (page not available), without a corresponding rescue result. The claim conflates the two mutants. (LLM, conf=0.86)
Experimental — accuracy not yet measuredUpon 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.
“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 [172]
The Results sections on phosphorylation of the F-actin-binding region report that Ca2+/CaM reduces CaMKIIβ binding to F-actin and that autophosphorylation in that region prevents binding from recovering after Ca2+ chelation (page not provided). But the paper describes competition as a possible steric-hindrance mechanism involving adjacent binding domains, not an established competition for the same F-actin-binding region. (LLM, conf=0.88)
Experimental — accuracy not yet measuredDeletion of CaMKIIβ impairs LTP, as does deletion of CaMKIIα.
“Interestingly, deletion of CaMKIIβ impairs LTP (121, 172, 175), as does the deletion of CaMKIIα.”
From Synaptic memory and CaMKII (2023) · cites this paper as [172]
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- Authors
- Kim, K., Lakhanpal, G., Lu, H. E., Khan, M., Suzuki, A., Kato Hayashi, M., Narayanan, R., Luyben, T. T., Matsuda, T., Nagai, T., Blanpied, T. A., Hayashi, Y., & Okamoto, K.
- Affiliations
- RIKEN Center for Brain Science (JP)
- Mount Sinai Hospital (CA)
- University of Maryland, Baltimore (US)
- Massachusetts Institute of Technology (US)
- The Institute of Scientific and Industrial Research, The University of Osaka (JP)
- South China Normal University (CN)
- Corresponding author
- Hayashi, Yasunori
- Okamoto, Kenichi
- ORCID
- Venue
- Neuron
- Publisher
- Elsevier BV
- Published
- 2015-08
- Volume
- 87
- Issue
- 4
- Pages
- 813-826
- ISSN
- 0896-6273 (ISSN-L)
- PMC
- PMC4548268
- OpenAlex
- W1810244153
- Cited by
- 145
- References
- 47
- Citations by year
- 2026: 8 · 2025: 9 · 2024: 12 · 2023: 9 · 2022: 12 · 2021: 11 · 2020: 14 · 2019: 14 · 2018: 20 · 2017: 18 · 2016: 16 · 2015: 2
- FWCI
- 8.71
- Type
- journal article
- Language
- en
- Update notices
- erratum (2015-10-21)
- Open access
- bronze
- doi.org
- Licence
- Locations
- Neuron (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- Canadian Institutes of Health Research (MOP111220)
- Japan Society for the Promotion of Science (15K14330, 26251018)
- National Institute of Mental Health (R01MH080046, R37MH080046)
- National Institute on Drug Abuse (R01DA17310, 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, synaptic plasticity, dendritic spines, actin cytoskeleton remodeling, F-actin binding, autophosphorylation, spinal stabilization
- MeSH terms
- Actins, Animals, Cells, Cultured, Chlorocebus aethiops, Neuronal Plasticity, Organ Culture Techniques, Protein Binding, COS Cells, Dendritic Spines, Rats, Calcium-Calmodulin-Dependent Protein Kinase Type 2
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