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CaMKII Autophosphorylation Is Necessary for Optimal Integration of Ca 2+ Signals during LTP Induction, but Not Maintenance
Open accessAbstract
CaMKII plays a critical role in decoding calcium (Ca 2+) signals to initiate long-lasting synaptic plasticity. However, the properties of CaMKII that mediate Ca 2+ signals in spines remain elusive. Here, we measured CaMKII activity in spines using fast-framing two-photon fluorescence lifetime imaging. Following each pulse during repetitive Ca 2+ elevations, CaMKII activity increased in a stepwise manner. Thr286 phosphorylation slows the decay of CaMKII and thus lowers the frequency required to induce spine plasticity by several fold. In the absence of Thr286 phosphorylation, increasing the stimulation frequency results in high peak mutant CaMKII T286A activity that is sufficient for inducing plasticity. Our findings demonstrate that Thr286 phosphorylation plays an important role in induction of LTP by integrating Ca 2+ signals, and it greatly promotes, but is dispensable for, the activation of CaMKII and LTP.
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“In essence, T286 autophosphorylation and CaM trapping would produce a frequency dependence for CaMKII activation.”
From Synaptic memory and CaMKII (2023) · cites this paper as [94]
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“This representation is strikingly similar to actual CaMKII responses in synaptic spines stimulated by repetitive glutamate uncaging and, as in FIGURE 3, shows little integrated activation with T286A CaMKII, unless substantially higher frequencies are used (94).”
From Synaptic memory and CaMKII (2023) · cites this paper as [94]
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“Despite these findings suggesting a critical role of T286, it should be noted that Chang et al. (94) reported that LTP can be expressed in the absence of T286 phosphorylation.”
From Synaptic memory and CaMKII (2023) · cites this paper as [94]
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Metadata
- Authors
- Chang, J.-Y., Parra-Bueno, P., Laviv, T., Szatmari, E. M., Lee, S.-J. R., & Yasuda, R.
- Affiliations
- Duke University (US)
- Max Planck Florida Institute for Neuroscience (US)
- Duke Medical Center (US)
- Corresponding author
- Yasuda, Ryohei
- Venue
- Neuron
- Publisher
- Elsevier BV
- Published
- 2017-05
- Volume
- 94
- Issue
- 4
- Pages
- 800-808.e4
- ISSN
- 0896-6273 (ISSN-L)
- PMC
- PMC5573161
- OpenAlex
- W2616355480
- Cited by
- 161
- References
- 44
- Citations by year
- 2026: 3 · 2025: 16 · 2024: 20 · 2023: 22 · 2022: 21 · 2021: 19 · 2020: 24 · 2019: 19 · 2018: 13 · 2017: 3
- FWCI
- 7.90
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Neuron (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- YUHSpace (Yonsei University Medical Library) (submittedVersion, cc-by-nc-nd)
- MPG.PuRe (Max Planck Society) (submittedVersion)
- Funders
- NIH (R01MH080047, 1DP1NS096787)
- 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 › Neuroscience › Cognitive Neuroscience › Memory and Neural Mechanisms
- Keywords
- CaMKII, autophosphorylation, long-term potentiation, calcium signaling, synaptic plasticity, dendritic spines, LTP maintenance, stimulation frequency
- MeSH terms
- Animals, Calcium, Hippocampus, Microscopy, Fluorescence, Neuronal Plasticity, Phosphorylation, Long-Term Potentiation, Pyramidal Cells, Patch-Clamp Techniques, Calcium Signaling, Mice, Calcium-Calmodulin-Dependent Protein Kinase Type 2, CA1 Region, Hippocampal
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