Deleterious Effects of Amyloid β Oligomers Acting as an Extracellular Scaffold for mGluR5

Renner, Marianne; Lacor, Pascale N.; Velasco, Pauline T.; Xu, Jian; Contractor, Anis; Klein, William L.; Triller, Antoine

doi:10.1016/j.neuron.2010.04.029

Cited by 468Alzheimer's disease research and treatmentsNeuroscience and Neuropharmacology ResearchNeuroinflammation and Neurodegeneration Mechanisms

Deleterious Effects of Amyloid β Oligomers Acting as an Extracellular Scaffold for mGluR5

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Renner, Marianne, Lacor, Pascale N., Velasco, Pauline T., Xu, Jian, Contractor, Anis, Klein, William L., Triller, Antoine·2010·Neuron

DOI 10.1016/j.neuron.2010.04.029PMC PMC3111138

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Abstract

Soluble oligomers of amyloid beta (Abeta) play a role in the memory impairment characteristic of Alzheimer's disease. Acting as pathogenic ligands, Abeta oligomers bind to particular synapses and perturb their function, morphology, and maintenance. Events that occur shortly after oligomer binding have been investigated here in live hippocampal neurons by single particle tracking of quantum dot-labeled oligomers and synaptic proteins. Membrane-attached oligomers initially move freely, but their diffusion is hindered markedly upon accumulation at synapses. Concomitantly, individual metabotropic glutamate receptors (mGluR5) manifest strikingly reduced lateral diffusion as they become aberrantly clustered. This clustering of mGluR5 elevates intracellular calcium and causes synapse deterioration, responses prevented by an mGluR5 antagonist. As expected, clustering by artificial crosslinking also promotes synaptotoxicity. These results reveal a mechanism whereby Abeta oligomers induce the abnormal accumulation and overstabilization of a glutamate receptor, thus providing a mechanistic and molecular basis for Abeta oligomer-induced early synaptic failure.

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Aβ oligomers can drive additional vicious cycles by stimulating metabotropic glutamate receptor 5 (mGluR5), which activates feedforward Ca2+-cAMP signaling and drives tau phosphorylation.
“Aβ oligomers can drive additional vicious cycles by stimulating metabotropic glutamate receptor 5 (mGluR5)146,147, which activates feedforward Ca2+–cAMP signaling and drive tau phosphorylation (Fig. 5, brown).”
From Stress weakens prefrontal networks: molecular insults to higher cognition (2015) · cites this paper as [146]
Aβ oligomers bind to α7 nicotinic acetylcholine receptors (α7 nAChRs) and to metabotropic glutamate receptors, in particular mGluR5.
“Aβ binds to α7 nicotinic acetylcholine receptors (α7 nAChRs) and to metabotropic glutamate receptors, in particular mGluR5 [31–33].”
From ApoE, ApoE Receptors, and the Synapse in Alzheimer's Disease (2017) · cites this paper as [32]
ADDL binding to synapses displays saturable kinetics.
“ADDL binding to synapses displays saturable kinetics (Renner et al., 2010)”
From The Aβ oligomer hypothesis for synapse failure and memory loss in Alzheimer’s disease (2011) · cites this paper as Renner et al., 2010
Double-labeling with synaptophysin or FM463 establishes oligomer localization to be at functional synapses.
“Double-labeling with synaptophysin or FM463 establishes this localization to be at functional synapses (Renner et al., 2010).”
From The Aβ oligomer hypothesis for synapse failure and memory loss in Alzheimer’s disease (2011) · cites this paper as Renner et al., 2010
Metabotropic glutamate receptors (mGluR5) participate in oligomer binding and clustering at synapses.
“single particle tracking of quantum dot-labeled Aβ oligomers has demonstrated the participation of metabotropic glutamate receptors (mGluR5) in oligomer binding and clustering at synapses (Renner et al., 2010).”
From The Aβ oligomer hypothesis for synapse failure and memory loss in Alzheimer’s disease (2011) · cites this paper as Renner et al., 2010

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Authors: Renner, M., Lacor, P. N., Velasco, P. T., Xu, J., Contractor, A., Klein, W. L., & Triller, A.
Affiliations: Centre National de la Recherche Scientifique (FR)
Northwestern University (US)
Corresponding author: Klein, William L.
Triller, Antoine
ORCID: Renner, Marianne
Xu, Jian
Contractor, Anis
Klein, William L.
Triller, Antoine
Venue: Neuron
Publisher: Elsevier BV
Published: 2010-06
Volume: 66
Issue: 5
Pages: 739-754
ISSN: 0896-6273 (ISSN-L)
DOI: 10.1016/j.neuron.2010.04.029
PMC: PMC3111138
OpenAlex: W2003655335
Cited by: 468
References: 62
Citations by year: 2026: 18 · 2025: 22 · 2024: 23 · 2023: 14 · 2022: 26 · 2021: 34 · 2020: 38 · 2019: 25 · 2018: 29 · 2017: 26 · 2016: 32 · 2015: 38 · 2014: 31 · 2013: 30 · 2012: 44
FWCI: 24.27
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, 1142 d)
Locations: Neuron (publishedVersion)
PubMed (publishedVersion)
PubMed Central (acceptedVersion)
HAL (submittedVersion, cc-by-nc)
Funders: National Institute on Aging (R01AG029460)
National Institute of Neurological Disorders and Stroke (R01NS058894)
Topics: Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
Keywords: amyloid-beta oligomers, mGluR5, metabotropic glutamate receptors, receptor clustering, synaptic dysfunction, synaptotoxicity, Alzheimer's disease, hippocampal neurons, single-particle tracking, quantum dots, intracellular calcium, receptor diffusion, receptor cross-linking
MeSH terms: Animals, Cells, Cultured, Extracellular Matrix, Neurons, Protein Binding, Synapses, Amyloid beta-Peptides, Rats, Sprague-Dawley, Receptors, Metabotropic Glutamate, Mice, Knockout, Mice, Rats, Protein Stability, Receptor, Metabotropic Glutamate 5

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Deleterious Effects of Amyloid β Oligomers Acting as an Extracellular Scaffold for mGluR5

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