The DOI matches its Crossref record; 15 of the 15 references it cites were found in a registry or an index.
A developmental switch in the signaling cascades for LTP induction
Abstract
Long-term potentiation (LTP) is thought to be critically involved not only in learning and memory, but also during the activity-dependent developmental phases of neural circuit formation and refinement. Whether the mechanisms underlying LTP change during this phase of postnatal development, however, is unknown. We report here that, unlike LTP in the more mature CA1 region of the hippocampus, LTP in neonatal rodent hippocampus (<9 postnatal days, <P9) requires cyclic AMP-dependent protein kinase A (PKA) but not Ca(2+)/calmodulin-dependent protein kinase II (CaMKII).
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In the citing paper
“Foremost are data, now long accepted, that NMDAR-dependent LTP is greatly impaired when T286 is replaced by T286A (43, 121, 381–384).”
From Synaptic memory and CaMKII (2023) · cites this paper as [381]
In the citing paper
“The period of early postnatal life when GluA4 is expressed also coincides with a period where PKA, and not CaMKII, is required for hippocampal LTP (Yasuda et al., 2003).”
From The AMPA Receptor Code of Synaptic Plasticity (2018) · cites this paper as Yasuda et al., 2003
Citations
Cites
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Long-Term Potentiation--A Decade of Progress?
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Self-citationThe molecular basis of CaMKII function in synaptic and behavioural memory
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Autophosphorylation at Thr 286 of the α Calcium-Calmodulin Kinase II in LTP and Learning
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Molecular Psychology: Roles for the ERK MAP Kinase Cascade in Memory
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Postsynaptic CAMP pathway gates early LTP in hippocampal CA1 region
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Malenka, R. C., & Bear, M. F. (2004) · Neuron · doi:10.1016/j.neuron.2004.09.012 · Cited by 3,968
Self-citationAMPA receptor trafficking at excitatory synapses
Bredt, D. S., & Nicoll, R. A. (2003) · Neuron · doi:10.1016/s0896-6273(03)00640-8 · Cited by 1,150
Mitogen-activated protein kinases in synaptic plasticity and memory
Sweatt, J. D. (2004) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2004.04.001 · Cited by 1,013
PKA phosphorylation of AMPA receptor subunits controls synaptic trafficking underlying plasticity
Esteban, J. A., Shi, S.-H., Wilson, C., Nuriya, M., Huganir, R. L., & Malinow, R. (2003) · Nature Neuroscience · doi:10.1038/nn997 · Cited by 894
The AMPA Receptor Code of Synaptic Plasticity
Diering, G. H., & Huganir, R. L. (2018) · Neuron · doi:10.1016/j.neuron.2018.10.018 · Cited by 844
Metadata
- Authors
- Yasuda, H., Barth, A. L., Stellwagen, D., & Malenka, R. C.
- Affiliations
- Stanford Medicine (US)
- Corresponding author
- Malenka, Robert C.
- Venue
- Nature Neuroscience
- Published
- 2002-12-02
- Volume
- 6
- Issue
- 1
- Pages
- 15-16
- ISSN
- 1097-6256 (ISSN-L)
- 1546-1726
- OpenAlex
- W2077306952
- Cited by
- 325
- References
- 15
- Citations by year
- 2025: 5 · 2024: 7 · 2023: 6 · 2022: 9 · 2021: 9 · 2020: 9 · 2019: 15 · 2018: 7 · 2017: 11 · 2016: 15 · 2015: 18 · 2014: 11 · 2013: 14 · 2012: 17
- FWCI
- 5.46
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Neuroscience (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Life Sciences › Neuroscience › Cognitive Neuroscience › Memory and Neural Mechanisms
- Life Sciences › Neuroscience › Developmental Neuroscience › Neurogenesis and neuroplasticity mechanisms
- Keywords
- long-term potentiation, developmental switch, signaling pathways, neonatal hippocampus, CA1, postnatal development, neural circuit refinement, synaptic plasticity, learning and memory
- MeSH terms
- Animals, Animals, Newborn, Carrier Proteins, Dose-Response Relationship, Drug, Enzyme Inhibitors, Colforsin, Hippocampus, Mutation, Neural Pathways, Synaptic Transmission, Neurons, Peptide Fragments, Signal Transduction, Long-Term Potentiation, Cyclic AMP-Dependent Protein Kinases, Calcium-Calmodulin-Dependent Protein Kinases, Excitatory Postsynaptic Potentials, Mitogen-Activated Protein Kinase 1, Intracellular Signaling Peptides and Proteins, Rats, Calcium-Calmodulin-Dependent Protein Kinase Type 2
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