Cited by 350Neuroscience and Neuropharmacology ResearchProtein Kinase Regulation and GTPase SignalingSignaling Pathways in Disease

CaMKIIβ Functions As an F-Actin Targeting Module that Localizes CaMKIIα/β Heterooligomers to Dendritic Spines

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Shen, Kang, Teruel, Mary N, Subramanian, Kala, Meyer, Tobias·1998·Neuron

Abstract

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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Crossref · 10.1016/s0896-6273(00)80569-3

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  • Inactive CaMKIIβ, but not α, binds with high affinity to F-actin.

    “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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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
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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