High-Resolution Proteomics Unravel Architecture and Molecular Diversity of Native AMPA Receptor Complexes
Open accessAbstract
AMPA-type glutamate receptors (AMPARs) are responsible for a variety of processes in the mammalian brain including fast excitatory neurotransmission, postsynaptic plasticity, or synapse development. Here, with comprehensive and quantitative proteomic analyses, we demonstrate that native AMPARs are macromolecular complexes with a large molecular diversity. This diversity results from coassembly of the known AMPAR subunits, pore-forming GluA and three types of auxiliary proteins, with 21 additional constituents, mostly secreted proteins or transmembrane proteins of different classes. Their integration at distinct abundance and stability establishes the heteromultimeric architecture of native AMPAR complexes: a defined core with a variable periphery resulting in an apparent molecular mass between 0.6 and 1 MDa. The additional constituents change the gating properties of AMPARs and provide links to the protein dynamics fundamental for the complex role of AMPARs in formation and operation of glutamatergic synapses.
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AMPARs are decorated by auxiliary subunits that control their synthesis, trafficking, and biophysical properties.
“Evidence has accumulated over the past decade indicating that AMPARs are not stand-alone receptors; rather, they are decorated by numerous types of auxiliary subunits that control the synthesis, trafficking, and biophysical properties of these receptors (278–281).”
From Synaptic memory and CaMKII (2023) · cites this paper as [281]
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- Authors
- Schwenk, J., Harmel, N., Brechet, A., Zolles, G., Berkefeld, H., Müller, C. S., Bildl, W., Baehrens, D., Hüber, B., Kulik, A., Klöcker, N., Schulte, U., & Fakler, B.
- Affiliations
- University of Freiburg (DE)
- Heinrich Heine University Düsseldorf (DE)
- Corresponding author
- Schulte, Uwe
- Fakler, Bernd
- Venue
- Neuron
- Publisher
- Elsevier BV
- Published
- 2012-05
- Volume
- 74
- Issue
- 4
- Pages
- 621-633
- ISSN
- 0896-6273 (ISSN-L)
- OpenAlex
- W2004277471
- Cited by
- 433
- References
- 66
- Citations by year
- 2026: 21 · 2025: 23 · 2024: 26 · 2023: 30 · 2022: 28 · 2021: 45 · 2020: 36 · 2019: 24 · 2018: 43 · 2017: 43 · 2016: 37 · 2015: 28 · 2014: 23 · 2013: 23 · 2012: 3
- FWCI
- 10.15
- 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, 478 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)
- Funders
- Deutsche Forschungsgemeinschaft (SFB 746/TP16, SFB780/A2, SFB780/A3)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Amino Acid Enzymes and Metabolism
- Keywords
- AMPA receptors, auxiliary proteins, secreted proteins, transmembrane proteins, receptor gating, glutamatergic synapses, excitatory neurotransmission, postsynaptic plasticity, synaptic development
- MeSH terms
- Animals, Brain, Synaptic Transmission, Neurons, Protein Conformation, Synapses, Xenopus, Receptors, AMPA, Protein Subunits, Protein Transport, Proteomics, Mice, Rats
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