Cited by 223Neuroscience and Neuropharmacology ResearchCell Adhesion Molecules ResearchGenetics and Neurodevelopmental Disorders

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Activity-Dependent Regulation of Synaptic AMPA Receptor Composition and Abundance by β3 Integrins

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Cingolani, Lorenzo A., Thalhammer, Agnes, Yu, Lily M.Y., Catalano, Myriam, Ramos, Timothy, Colicos, Michael A., Goda, Yukiko·2008·Neuron

DOI 10.1016/j.neuron.2008.04.011PMC PMC2446609

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Abstract

At synapses, cell adhesion molecules (CAMs) provide the molecular framework for coordinating signaling events across the synaptic cleft. Among synaptic CAMs, the integrins, receptors for extracellular matrix proteins and counterreceptors on adjacent cells, are implicated in synapse maturation and plasticity and memory formation. However, little is known about the molecular mechanisms of integrin action at central synapses. Here, we report that postsynaptic beta3 integrins control synaptic strength by regulating AMPA receptors (AMPARs) in a subunit-specific manner. Pharmacological perturbation targeting beta3 integrins promotes endocytosis of GluR2-containing AMPARs via Rap1 signaling, and expression of beta3 integrins produces robust changes in the abundance and composition of synaptic AMPARs without affecting dendritic spine structure. Importantly, homeostatic synaptic scaling induced by activity deprivation elevates surface expression of beta3 integrins, and in turn, beta3 integrins are required for synaptic scaling. Our findings demonstrate a key role for integrins in the feedback regulation of excitatory synaptic strength.

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Authors: Cingolani, L. A., Thalhammer, A., Yu, L. M. Y., Catalano, M., Ramos, T., Colicos, M. A., & Goda, Y.
Affiliations: MRC Laboratory for Molecular Cell Biology (GB)
University College London (GB)
University of Calgary (CA)
Corresponding author: Cingolani, Lorenzo A.
Goda, Yukiko
ORCID: Cingolani, Lorenzo A.
Thalhammer, Agnes
Catalano, Myriam
Colicos, Michael A.
Goda, Yukiko
Venue: Neuron
Publisher: Elsevier BV
Published: 2008-06
Volume: 58
Issue: 5
Pages: 749-762
ISSN: 0896-6273 (ISSN-L)
DOI: 10.1016/j.neuron.2008.04.011
PMC: PMC2446609
OpenAlex: W1983897183
Cited by: 223
References: 70
Citations by year: 2026: 6 · 2025: 7 · 2024: 7 · 2023: 8 · 2022: 12 · 2021: 9 · 2020: 9 · 2019: 7 · 2018: 9 · 2017: 6 · 2016: 17 · 2015: 12 · 2014: 19 · 2013: 18 · 2012: 18
FWCI: 8.50
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 1872 d)
Locations: Neuron (publishedVersion)
PubMed (publishedVersion)
PubMed Central (acceptedVersion)
ArTS Archivio della ricerca di Trieste (University of Trieste https://www.units.it/) (submittedVersion)
UCL Discovery (University College London) (submittedVersion)
IRIS Research product catalog (Sapienza University of Rome) (submittedVersion)
Funders: National Institutes of Health
National Institute of Mental Health (R01MH066676, R01MH66676)
Topics: Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
Health Sciences › Medicine › Immunology and Allergy › Cell Adhesion Molecules Research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Genetics and Neurodevelopmental Disorders
Keywords: CD61, AMPA receptors, GluR2, Rap1 signaling, synaptic scaling, homeostatic plasticity, activity-dependent regulation, synaptic efficacy, receptor internalization, dendritic spines, excitatory synapses
MeSH terms: Animals, Chelating Agents, Egtazic Acid, Endocytosis, Gene Expression Regulation, Hippocampus, Neural Inhibition, Neurons, Peptides, Platelet Aggregation Inhibitors, Synapses, Time Factors, Transfection, Presynaptic Terminals, Receptors, AMPA, Mice, Knockout, Patch-Clamp Techniques, Excitatory Amino Acids, Bridged Bicyclo Compounds, Heterocyclic, Excitatory Postsynaptic Potentials, rap1 GTP-Binding Proteins, Intercellular Signaling Peptides and Proteins, Integrin beta3, Mice, Rats, Thiazolidines, In Vitro Techniques

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Activity-Dependent Regulation of Synaptic AMPA Receptor Composition and Abundance by β3 Integrins

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