Synaptic transmission and plasticity require AMPA receptor anchoring via its N-terminal domain
Open accessAbstract
AMPA-type glutamate receptors (AMPARs) mediate fast excitatory neurotransmission and are selectively recruited during activity-dependent plasticity to increase synaptic strength. A prerequisite for faithful signal transmission is the positioning and clustering of AMPARs at postsynaptic sites. The mechanisms underlying this positioning have largely been ascribed to the receptor cytoplasmic C-termini and to AMPAR-associated auxiliary subunits, both interacting with the postsynaptic scaffold. Here, using mouse organotypic hippocampal slices, we show that the extracellular AMPAR N-terminal domain (NTD), which projects midway into the synaptic cleft, plays a fundamental role in this process. This highly sequence-diverse domain mediates synaptic anchoring in a subunit-selective manner. Receptors lacking the NTD exhibit increased mobility in synapses, depress synaptic transmission and are unable to sustain long-term potentiation (LTP). Thus, synaptic transmission and the expression of LTP are dependent upon an AMPAR anchoring mechanism that is driven by the NTD.
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The amino terminal domain is not necessary for formation of functional ion channels, or delivery onto the cell surface, but is required for targeting and retention of GluA1 at synapses during LTP.
“Data show that the amino terminal domain is not necessary for the formation of functional ion channels, or delivery onto the cell surface, but is required for targeting and retention of GluA1 at synapses during LTP (Watson et al., 2017, Diaz-Alonso et al., 2017).”
From The AMPA Receptor Code of Synaptic Plasticity (2018) · cites this paper as Watson et al., 2017
The Results section ('GluA1 requires the NTD for synaptic delivery'; page unavailable) shows that GluA1 lacking its N-terminal domain produces surface currents but fails to incorporate effectively at synapses. The LTP Results and Discussion show that potentiation cannot be maintained without the domain. However, the Discussion also reports transient potentiation and apparent synaptic incorporation of GluA1 lacking the domain, so the claim that it is required for initial targeting during LTP is too strong. (LLM, conf=0.85)
Experimental — accuracy not yet measuredTagging GluA1 on the NH2 terminus severely impacts the trafficking of the GluA1-containing receptor.
“Third, most of these studies have tagged GluA1 on the NH2 terminus. This tagging severely impacts the trafficking of the GluA1-containing receptor (343, 344).”
From Synaptic memory and CaMKII (2023) · cites this paper as [343]
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Self-citationStructure and organization of AMPA receptor-TARP complexes in the mammalian cerebellum
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The functional impact of LGI1 autoantibodies on human CA3 pyramidal neurons
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- Authors
- Watson, J. F., Ho, H., & Greger, I. H.
- Affiliations
- MRC Laboratory of Molecular Biology (GB)
- Corresponding author
- Greger, Ingo H
- Venue
- eLife
- Publisher
- eLife Sciences Publications, Ltd
- Published
- 2017-03-14
- Volume
- 6
- ISSN
- 2050-084X (ISSN-L)
- PMC
- PMC5370185
- OpenAlex
- W2600278343
- Cited by
- 117
- References
- 74
- Citations by year
- 2026: 11 · 2025: 11 · 2024: 14 · 2023: 14 · 2022: 11 · 2021: 11 · 2020: 15 · 2019: 8 · 2018: 13 · 2017: 9
- FWCI
- 5.97
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- eLife (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion)
- Funders
- Medical Research Council (MC_U105174197)
- Biotechnology and Biological Sciences Research Council (BB/N002113/1)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nicotinic Acetylcholine Receptors Study
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Amino Acid Enzymes and Metabolism
- Keywords
- AMPA receptors, synaptic transmission, long-term potentiation, synaptic plasticity, receptor mobility, postsynaptic scaffolds, hippocampus
- MeSH terms
- Animals, Hippocampus, Synaptic Transmission, Receptors, AMPA, Mice
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