Extracellular interactions between GluR2 and N-cadherin in spine regulation
Open accessAbstract
Via its extracellular N-terminal domain (NTD), the AMPA receptor subunit GluR2 promotes the formation and growth of dendritic spines in cultured hippocampal neurons. Here we show that the first N-terminal 92 amino acids of the extracellular domain are necessary and sufficient for GluR2's spine-promoting activity. Moreover, overexpression of this extracellular domain increases the frequency of miniature excitatory postsynaptic currents (mEPSCs). Biochemically, the NTD of GluR2 can interact directly with the cell adhesion molecule N-cadherin, in cis or in trans. N-cadherin-coated beads recruit GluR2 on the surface of hippocampal neurons, and N-cadherin immobilization decreases GluR2 lateral diffusion on the neuronal surface. RNAi knockdown of N-cadherin prevents the enhancing effect of GluR2 on spine morphogenesis and mEPSC frequency. Our data indicate that in hippocampal neurons N-cadherin and GluR2 form a synaptic complex that stimulates presynaptic development and function as well as promoting dendritic spine formation.
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Cell adhesion complexes are diffusion barriers for membrane proteins.
“Cell adhesion complexes have also been identified as diffusion barriers for membrane proteins (O’Brien et al., 1999; Saglietti et al., 2007).”
From Barriers in the brain: resolving dendritic spine morphology and compartmentalization (2014) · cites this paper as Saglietti et al., 2007
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- Authors
- Saglietti, L., Dequidt, C., Kamieniarz, K., Rousset, M.-C., Valnegri, P., Thoumine, O., Beretta, F., Fagni, L., Choquet, D., Sala, C., Sheng, M., & Passafaro, M.
- Affiliations
- University of Milan (IT)
- Centre National de la Recherche Scientifique (FR)
- Institut de Génomique Fonctionnelle (FR)
- Howard Hughes Medical Institute (US)
- Corresponding author
- Passafaro, Maria
- ORCID
- Venue
- Neuron
- Publisher
- Elsevier BV
- Published
- 2007-05
- Volume
- 54
- Issue
- 3
- Pages
- 461-477
- ISSN
- 0896-6273 (ISSN-L)
- OpenAlex
- W2162281220
- Cited by
- 341
- References
- 2
- Citations by year
- 2026: 5 · 2025: 5 · 2024: 11 · 2023: 8 · 2022: 9 · 2021: 16 · 2020: 13 · 2019: 10 · 2018: 18 · 2017: 16 · 2016: 24 · 2015: 14 · 2014: 24 · 2013: 23 · 2012: 22
- FWCI
- 11.76
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- www.elsevier.com/legal/tdmrep-license (tdm)
- www.elsevier.com/open-access/userlicense/1.0/ (vor, 2305 d)
- doi.org/10.15223/policy-017 (stm-asf)
- doi.org/10.15223/policy-037 (stm-asf)
- doi.org/10.15223/policy-012 (stm-asf)
- doi.org/10.15223/policy-029 (stm-asf)
- doi.org/10.15223/policy-004 (stm-asf)
- Locations
- Neuron (publishedVersion)
- PubMed (publishedVersion)
- INFM-OAR (INFN Catania) (submittedVersion, other-oa)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Genetics and Neurodevelopmental Disorders
- Health Sciences › Medicine › Immunology and Allergy › Cell Adhesion Molecules Research
- Keywords
- GluR2, N-cadherin, AMPA receptors, dendritic spine formation, spine morphogenesis, adhesion molecules, synaptic complex, miniature excitatory postsynaptic currents, hippocampal neurons, receptor lateral diffusion, synaptic plasticity
- MeSH terms
- Animals, Cells, Cultured, Embryo, Mammalian, Extracellular Space, Hippocampus, Mutation, Nerve Tissue Proteins, Neurons, Spine, Transfection, Cadherins, Protein Structure, Tertiary, Receptors, AMPA, Patch-Clamp Techniques, Excitatory Postsynaptic Potentials, Protein Transport, RNA Interference, Green Fluorescent Proteins, Rats
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