Cited by 329Neuroscience and Neuropharmacology ResearchMemory and Neural MechanismsProtein Kinase Regulation and GTPase Signaling

Potentiated transmission and prevention of further LTP by increased CaMKII activity in postsynaptic hippocampal slice neurons

Pettit, D. L., Perlman, S., Malinow, R.·1994·Science

Abstract

Calcium-calmodulin-dependent protein kinase II (CaMKII) is a necessary component of the cellular machinery underlying learning and memory. Here, a constitutively active form of this enzyme, CaMKII(1-290), was introduced into neurons of hippocampal slices with a recombinant vaccinia virus to test the hypothesis that increased postsynaptic activity of this enzyme is sufficient to produce long-term synaptic potentiation (LTP), a prominent cellular model of learning and memory. Postsynaptic expression of CaMKII(1-290) increased CaMKII activity, enhanced synaptic transmission, and prevented more potentiation by an LTP-inducing protocol. These results, together with previous studies, suggest that postsynaptic CaMKII activity is necessary and sufficient to generate LTP.

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Crossref · 10.1126/science.7997883

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52 of 52 references verified0 citation errors · 0 not checkable

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  • Calcium ions play a crucial role in initiating downstream signaling during long-term potentiation (LTP) and depression (LTD) and influx of calcium is both necessary and sufficient for structural synaptic plasticity.

    “Calcium ions play a crucial role in initiating downstream signaling during long-term potentiation (LTP) and depression (LTD) and influx of calcium is both necessary and sufficient for structural synaptic plasticity (Pettit et al., 1994; Lledo et al., 1995; Otmakhov et al., 2004).”
  • CaMKII occludes LTP.

    “This is indeed the case (199, 209).”

    From Synaptic memory and CaMKII (2023) · cites this paper as [209]

  • Expression of active CaMKII or direct delivery into the cell via the recording electrode has repeatedly revealed a roughly two- to threefold enhancement in the AMPAR EPSC but little change in the NMDAR EPSC.

    “Expression of active CaMKII (121, 130–132, 209, 210, 212) or direct delivery into the cell via the recording electrode (199) has repeatedly revealed a roughly two- to threefold enhancement in the AMPAR EPSC but little change in the NMDAR EPSC (130–132).”

    From Synaptic memory and CaMKII (2023) · cites this paper as [209]

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Authors
Pettit, D. L., Perlman, S., & Malinow, R.
Affiliations
University of Iowa (US)
Venue
Science
Published
1994-12-16
Volume
266
Issue
5192
Pages
1881-1885
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W2076782463
Cited by
329
References
52
Citations by year
2026: 4 · 2025: 3 · 2024: 7 · 2023: 8 · 2022: 9 · 2021: 6 · 2020: 2 · 2019: 3 · 2018: 3 · 2017: 5 · 2016: 7 · 2015: 8 · 2014: 6 · 2013: 11 · 2012: 16
FWCI
6.55
Type
journal article
Language
en
Open access
closed
Locations
  • Science (publishedVersion)
  • PubMed (publishedVersion)
  • Cold Spring Harbor Laboratory Institutional Repository (Cold Spring Harbor Laboratory) (acceptedVersion)
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 transmission, hippocampal neurons, postsynaptic activity, learning and memory, synaptic plasticity, recombinant vaccinia virus
MeSH terms
Animals, Cell Line, Genetic Vectors, Hippocampus, Membrane Potentials, Synaptic Transmission, Recombinant Proteins, Transfection, Vaccinia virus, 2-Amino-5-phosphonovalerate, Long-Term Potentiation, Calcium-Calmodulin-Dependent Protein Kinases, Pyramidal Cells, Patch-Clamp Techniques, Rats, Calcium-Calmodulin-Dependent Protein Kinase Type 2, In Vitro Techniques

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