Cited by 92Neuroscience and Neuropharmacology ResearchCellular transport and secretionReceptor Mechanisms and Signaling

Plasma membrane insertion of the AMPA receptor GluA2 subunit is regulated by NSF binding and Q/R editing of the ion pore

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Araki, Yoichi, Lin, Da-Ting, Huganir, Richard L.·2010·Proceedings of the National Academy of Sciences

Abstract

The delivery of AMPA receptors to the plasma membrane is a critical step both for the synaptic delivery of these receptors and for the regulation of synaptic transmission. To directly visualize fusion events of transport vesicles containing the AMPA receptor GluA2 subunit with the plasma membrane we used pHluorin-tagged GluA2 subunits and total internal reflection fluorescence microscopy. We demonstrate that the plasma membrane insertion of GluA2 requires the NSF binding site within its intracellular cytoplasmic domain and that RNA editing of the Q/R site in the ion channel region plays a key role in GluA2 plasma membrane insertion. Finally, we show that plasma membrane insertion of heteromeric GluA2/3 receptors follows the same rules as homomeric GluA2 receptors. These results demonstrate that the plasma membrane delivery of GluA2 containing AMPA receptors is regulated by its unique structural elements.

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Crossref · 10.1073/pnas.1006584107

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  • GluA2-containing receptors (likely GluA2/3 heteromers) undergo spontaneous and constitutive exocytosis, but these events are much smaller, containing an estimated 2-5 receptors.

    “GluA2-containing receptors (likely GluA2/3 heteromers) undergo spontaneous and constitutive exocytosis, but these events are much smaller, containing an estimated 2-5 receptors (Araki et al., 2010, Gu et al., 2016, Lin et al., 2009).”

    From The AMPA Receptor Code of Synaptic Plasticity (2018) · cites this paper as Araki et al., 2010

    The Discussion reports that GluA2 exocytosis is largely constitutive (approximately 70%) and that its insertion events contain only a few receptors compared with GluA1; it also discusses GluA2/3 heteromers. The Results report lower fluorescence intensity for GluA2 events, but our copy does not give the claimed estimate of 2–5 receptors per event. (LLM, conf=0.87)

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Authors
Araki, Y., Lin, D.-T., & Huganir, R. L.
Affiliations
Howard Hughes Medical Institute (US)
Venue
Proceedings of the National Academy of Sciences
Published
2010-06
Volume
107
Issue
24
Pages
11080-11085
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W2083767904
Cited by
92
References
37
Citations by year
2026: 1 · 2025: 6 · 2024: 6 · 2023: 3 · 2022: 4 · 2021: 5 · 2020: 4 · 2019: 4 · 2018: 8 · 2017: 7 · 2016: 7 · 2015: 3 · 2014: 10 · 2013: 6 · 2012: 7
FWCI
3.11
Type
journal article
Language
en
Open access
Locations
  • Proceedings of the National Academy of Sciences (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
Funders
  • Howard Hughes Medical Institute
  • National Institute of Neurological Disorders and Stroke (R01NS036715)
Topics
  • Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
Keywords
AMPA receptors, GluR2 subunit, plasma membrane insertion, RNA editing, ion channel pore, vesicle fusion
MeSH terms
Amino Acid Sequence, Animals, Base Sequence, Binding Sites, Cell Membrane, Cells, Cultured, Hippocampus, Molecular Sequence Data, Neuronal Plasticity, Neurons, Recombinant Proteins, RNA Editing, DNA Primers, Receptors, AMPA, Protein Subunits, Rats, N-Ethylmaleimide-Sensitive Proteins, Protein Multimerization

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