The DOI matches its Crossref record; 60 of the 61 references it cites were found in a registry or an index.
CaMKIIβ Functions As an F-Actin Targeting Module that Localizes CaMKIIα/β Heterooligomers to Dendritic Spines
Open accessAbstract
Ca2+/calmodulin-dependent protein kinase II (CaMKII) is a serine/threonine protein kinase that regulates long-term potentiation and other forms of neuronal plasticity. Functional differences between the neuronal CaMKIIalpha and CaMKIIbeta isoforms are not yet known. Here, we use green fluorescent protein-tagged (GFP-tagged) CaMKII isoforms and show that CaMKIIbeta is bound to F-actin in dendritic spines and cell cortex while CaMKIIalpha is largely a cytosolic enzyme. When expressed together, the two isoforms form large heterooligomers, and a small fraction of CaMKIIbeta is sufficient to dock the predominant CaMKIIalpha to the actin cytoskeleton. Thus, CaMKIIbeta functions as a targeting module that localizes a much larger number of CaMKIIalpha isozymes to synaptic and cytoskeletal sites of action.
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“A second difference is the specific high-affinity binding of the inactive β, but not α, to F-actin (167–170).”
From Synaptic memory and CaMKII (2023) · cites this paper as [168]
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Cites
Control of memory formation through regulated expression of a CaMKII transgene
Mayford, M., Bach, M. E., Huang, Y.-Y., Wang, L., Hawkins, R. D., & Kandel, E. R. (1996) · Science · doi:10.1126/science.274.5293.1678 · Cited by 1,550
Deficient Hippocampal Long-Term Potentiation in α-Calcium-Calmodulin Kinase II Mutant Mice
Silva, A. J., Stevens, C. F., Tonegawa, S., & Wang, Y. (1992) · Science · doi:10.1126/science.1378648 · Cited by 1,472
Sensitivity of CaM Kinase II to the Frequency of Ca 2+ Oscillations
De Koninck, P., & Schulman, H. (1998) · Science · doi:10.1126/science.279.5348.227 · Cited by 1,269
Autophosphorylation at Thr 286 of the α Calcium-Calmodulin Kinase II in LTP and Learning
Giese, K. P., Fedorov, N. B., Filipkowski, R. K., & Silva, A. J. (1998) · Science · doi:10.1126/science.279.5352.870 · Cited by 1,055
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
Rapid Actin-Based Plasticity in Dendritic Spines
Fischer, M., Kaech, S., Knutti, D., & Matus, A. (1998) · Neuron · doi:10.1016/s0896-6273(00)80467-5 · Cited by 905
Evidence for a Role of Dendritic Filopodia in Synaptogenesis and Spine Formation
Ziv, N. E., & Smith, S. J. (1996) · Neuron · doi:10.1016/s0896-6273(00)80283-4 · Cited by 882
Miller, S. (1986) · Cell · doi:10.1016/0092-8674(86)90008-5 · Cited by 864
Contrasting properties of two forms of long-term potentiation in the hippocampus
Nicoll, R. A., & Malenka, R. C. (1995) · Nature · doi:10.1038/377115a0 · Cited by 861
The Multifunctional Calcium/Calmodulin-Dependent Protein Kinase: From Form to Function
Braun, A. P., & Schulman, H. (1995) · Annual Review of Physiology · doi:10.1146/annurev.ph.57.030195.002221 · Cited by 820
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Han, B., Zhao, Y., Yao, J., Li, N., Fang, T., Wang, Y., Meng, Z., & Liu, W. (2022) · SSRN Electronic Journal · doi:10.2139/ssrn.4098464
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Earl, D. E. (2011) · OhioLink ETD Center (Ohio Library and Information Network)
Metadata
- Authors
- Shen, K., Teruel, M. N., Subramanian, K., & Meyer, T.
- Affiliations
- Duke Medical Center (US)
- Corresponding author
- Meyer, Tobias
- Venue
- Neuron
- Publisher
- Elsevier BV
- Published
- 1998-09
- Volume
- 21
- Issue
- 3
- Pages
- 593-606
- ISSN
- 0896-6273 (ISSN-L)
- OpenAlex
- W2146831587
- Cited by
- 350
- References
- 61
- Citations by year
- 2026: 7 · 2025: 4 · 2024: 5 · 2023: 9 · 2022: 9 · 2021: 6 · 2020: 20 · 2019: 14 · 2018: 18 · 2017: 10 · 2016: 7 · 2015: 12 · 2014: 9 · 2013: 21 · 2012: 14
- FWCI
- 5.41
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Neuron (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (2r01gm051457-04)
- National Institute of General Medical Sciences (GM-48113, GM 51457)
- 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 › Molecular Biology › Signaling Pathways in Disease
- Keywords
- CaMKIIβ, CaMKIIα, CaMKII isoforms, hetero-oligomers, F-actin binding, dendritic spines, actin cytoskeleton, protein localization, synaptic plasticity, long-term potentiation, neuroplasticity
- MeSH terms
- Actins, Animals, Cloning, Molecular, Cytoskeleton, Dendrites, Isoenzymes, Luminescent Proteins, Nerve Fibers, Neurons, Phosphorylation, Recombinant Fusion Proteins, Synapses, Transcription, Genetic, Protein Biosynthesis, Tumor Cells, Cultured, 3T3 Cells, Calcium-Calmodulin-Dependent Protein Kinases, Macromolecular Substances, Green Fluorescent Proteins, Mice, Rats, Calcium-Calmodulin-Dependent Protein Kinase Type 2
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