CaMKIIβ binding to stable F-actin in vivo regulates F-actin filament stability
Open accessAbstract
Ca2 + /calmodulin-dependent protein kinase II (CaMKII) is a serine/threonine kinase that is best known for its role in synaptic plasticity and memory. Multiple roles of CaMKII have been identified in the hippocampus, yet its role in developing neurons is less well understood. We show here that endogenous CaMKIIβ, but not CaMKIIα, localized to prominent F-actin-rich structures at the soma in embryonic cortical neurons. Fluorescence recovery after photobleaching analyses of GFP-CaMKIIβ binding interactions with F-actin in this CaMKIIα-free system indicated CaMKIIβ binding depended upon a putative F-actin binding domain in the variable region of CaMKIIβ. Furthermore, CaMKIIα decreased CaMKIIβ binding to F-actin. We examined the interaction of CaMKIIβ with stable and dynamic actin and show that CaMKIIβ binding to F-actin was dramatically prolonged when F-actin was stabilized. CaMKIIβ binding to stable F-actin was disrupted when it was bound by Ca2 + /calmodulin or when it was highly phosphorylated, but not by kinase inactivity. Whereas CaMKIIβ over-expression increased the prevalence of the F-actin-rich structures, disruption of CaMKIIβ binding to F-actin reduced them. Taken together, these data suggest that CaMKIIβ binding to stable F-actin is important for the in vivo maintenance of polymerized F-actin.
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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 [167]
The Results report that CaMKIIβ bound strongly to stabilized F-actin whereas CaMKIIα did not; the Discussion says inactive CaMKIIβ binds F-actin and activation reduces binding strength. The claim omits the stable-F-actin condition: the Results found weaker binding to dynamic F-actin. (LLM, conf=0.85)
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Effects of Camk2b Overexpression and Underexpression on the Proteome of Rat Hippocampal Neurons
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Dephosphorylation-dependent Inhibitory Activity of Juxtanodin on Filamentous Actin Disassembly
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- Authors
- Lin, Y.-C., & Redmond, L.
- Affiliations
- Augusta University (US)
- ORCID
- Lin, Yu-Chih
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2008-10-14
- Volume
- 105
- Issue
- 41
- Pages
- 15791-15796
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC2572980
- OpenAlex
- W2032715957
- Cited by
- 96
- References
- 28
- Citations by year
- 2026: 2 · 2025: 2 · 2024: 3 · 2023: 6 · 2022: 5 · 2021: 2 · 2020: 5 · 2019: 6 · 2018: 7 · 2017: 4 · 2016: 7 · 2015: 7 · 2014: 8 · 2013: 5 · 2012: 8
- FWCI
- 2.61
- 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)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular Mechanics and Interactions
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Keywords
- CaMKIIβ, CaMKIIα, F-actin, actin filament stability, actin-binding domain, embryonic cortical neurons, Ca2+-calmodulin, protein phosphorylation, kinase activity, neuronal soma, hippocampus
- MeSH terms
- Actins, Animals, Cerebral Cortex, Embryo, Mammalian, Actin Cytoskeleton, Neurons, Protein Binding, Calcium-Calmodulin-Dependent Protein Kinase Type 2
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