Cited by 1,524Neuroscience and Neuropharmacology ResearchGenetics and Neurodevelopmental DisordersMemory and Neural Mechanisms

Driving AMPA receptors into synapses by LTP and CaMKII: requirement for GluR1 and PDZ domain interaction

Hayashi, Yasunori, Shi, Song-Hai, Esteban, José A., Piccini, Antonella, Poncer, Jean-Christophe, Malinow, Roberto·2000·Science

Abstract

To elucidate mechanisms that control and execute activity-dependent synaptic plasticity, alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate receptors (AMPA-Rs) with an electrophysiological tag were expressed in rat hippocampal neurons. Long-term potentiation (LTP) or increased activity of the calcium/calmodulin-dependent protein kinase II (CaMKII) induced delivery of tagged AMPA-Rs into synapses. This effect was not diminished by mutating the CaMKII phosphorylation site on the GluR1 AMPA-R subunit, but was blocked by mutating a predicted PDZ domain interaction site. These results show that LTP and CaMKII activity drive AMPA-Rs to synapses by a mechanism that requires the association between GluR1 and a PDZ domain protein.

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Crossref · 10.1126/science.287.5461.2262

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2 of 2 references verified0 citation errors · 0 not checkable

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  • The prevailing model posits that LTP-mediated covalent modification of the intracellular CTD of GluA1 results in capture of modified GluA1-containing receptors by preexisting slots in the PSD.

    “The prevailing model posits that LTP-mediated covalent modification of the intracellular CTD of GluA1 results in the capture of these modified GluA1-containing receptors by preexisting “slots” in the postsynaptic density (PSD) (17, 18, 212).”

    From Synaptic memory and CaMKII (2023) · cites this paper as [212]

  • Long-tailed AMPARs are recruited to synapses in an activity-dependent manner, while short-tailed AMPARs undergo constitutive cycling in and out of synapses.

    “Earlier studies suggest that long-tailed AMPARs are recruited to synapses in an activity-dependent manner, while short-tailed AMPARs undergo constitutive cycling in and out of synapses (Shi et al., 2001, Hayashi et al., 2000).”

    From The AMPA Receptor Code of Synaptic Plasticity (2018) · cites this paper as Hayashi et al., 2000

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Authors
Hayashi, Y., Shi, S.-H., Esteban, J. A., Piccini, A., Poncer, J.-C., & Malinow, R.
Affiliations
Cold Spring Harbor Laboratory (US)
Corresponding author
  • Hayashi, Yasunori
  • Shi, Song-Hai
  • Poncer, Jean-Christophe
  • Malinow, Roberto
Venue
Science
Published
2000-03-24
Volume
287
Issue
5461
Pages
2262-2267
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W1979586675
Cited by
1,524
References
2
Citations by year
2026: 17 · 2025: 24 · 2024: 31 · 2023: 26 · 2022: 30 · 2021: 54 · 2020: 35 · 2019: 47 · 2018: 61 · 2017: 45 · 2016: 49 · 2015: 54 · 2014: 83 · 2013: 68 · 2012: 70
FWCI
31.33
Type
journal article
Language
en
Open access
closed
Locations
  • Science (publishedVersion)
  • PubMed (publishedVersion)
  • Cold Spring Harbor Laboratory Institutional Repository (Cold Spring Harbor Laboratory) (acceptedVersion)
  • DIGITAL.CSIC (Spanish National Research Council (CSIC)) (submittedVersion)
Topics
  • Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Genetics and Neurodevelopmental Disorders
  • Life Sciences › Neuroscience › Cognitive Neuroscience › Memory and Neural Mechanisms
Keywords
AMPA receptors, GluR1, PDZ domain, CaMKII, long-term potentiation, synaptic plasticity, CaMKII phosphorylation, hippocampal neurons
MeSH terms
Animals, Cell Line, Hippocampus, Humans, Membrane Potentials, Mutation, Synaptic Transmission, Organ Culture Techniques, Phosphorylation, Proteins, Recombinant Fusion Proteins, Synapses, Protein Structure, Tertiary, Long-Term Potentiation, Calcium-Calmodulin-Dependent Protein Kinases, Pyramidal Cells, Receptors, AMPA, Patch-Clamp Techniques, Catalytic Domain, Rats, Calcium-Calmodulin-Dependent Protein Kinase Type 2

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