Synaptic memory survives molecular turnover
Open accessAbstract
Activation of Ca 2+ /calmodulin-dependent kinase II (CaMKII) plays a critical role in long-term potentiation (LTP), a long accepted cellular model for learning and memory. However, how LTP and memories survive the turnover of synaptic proteins, particularly CaMKII, remains a mystery. Here, we take advantage of the finding that constitutive Ca 2+ -independent CaMKII activity, acquired prior to slice preparation, provides a lasting memory trace at synapses. In slice culture, this persistent CaMKII activity, in the absence of Ca 2+ stimulation, remains stable over a 2-wk period, well beyond the turnover of CaMKII protein. We propose that the nascent CaMKII protein present at 2 wk acquired its activity from preexisting active CaMKII molecules, which transferred their activity to newly synthesized CaMKII molecules and thus maintain the memory in the face of protein turnover.
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Persistent CaMKII activity in the absence of Ca2+ stimulation remains stable over a 2-week period in hippocampal slice cultures.
“Persistent CaMKII activity, in the absence of Ca2+ stimulation, remains stable over a 2-wk period.”
From Synaptic memory and CaMKII (2023) · cites this paper as [413]
The nascent CaMKII protein present at 2 weeks acquired its activity from preexisting active CaMKII molecules, transferring their activity to newly synthesized CaMKII molecules and thus maintaining memory in the face of protein turnover.
“These results suggest that the nascent CaMKII protein present at 2 wk acquired its activity from preexisting active CaMKII molecules, transferring their activity to newly synthesized CaMKII molecules and thus maintaining the memory in the face of protein turnover.”
From Synaptic memory and CaMKII (2023) · cites this paper as [413]
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- Authors
- Lee, J., Chen, X., & Nicoll, R. A.
- Affiliations
- University of California, San Francisco (US)
- Corresponding author
- Nicoll, Roger A.
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2022-10-10
- Volume
- 119
- Issue
- 42
- Pages
- e2211572119-e2211572119
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC9586278
- OpenAlex
- W4304098632
- Cited by
- 27
- References
- 53
- Citations by year
- 2026: 2 · 2025: 7 · 2024: 8 · 2023: 8 · 2022: 2
- FWCI
- 2.76
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- National Institute of Mental Health and Neurosciences (R01MH117139)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Life Sciences › Neuroscience › Cognitive Neuroscience › Memory and Neural Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Keywords
- CaMKII, long-term potentiation, synaptic memory, protein turnover, constitutive kinase activity, memory traces, synaptic plasticity, learning and memory, slice culture
- MeSH terms
- Calmodulin, Hippocampus, Learning, Phosphorylation, Synapses, Long-Term Potentiation, Calcium-Calmodulin-Dependent Protein Kinase Type 2
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