ArticleThe Journal of biological chemistry2016
Proteomic Characterization of Inhibitory Synapses Using a Novel pHluorin-tagged γ-Aminobutyric Acid Receptor, Type A (GABAA), α2 Subunit Knock-in Mouse.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed, 56 citations in OpenAlex.
- Revealing acute consequences of rapid degradation of synaptic fusion proteins at individual synapses using Auxin-Inducible Degron 2 technology.Communications biology · 2025Article
- Milestone Review: Unlocking the Proteomics of Glycine Receptor Complexes.Journal of neurochemistry · 2025Review
- The brain-specific kinase LMTK3 regulates neuronal excitability by decreasing KCC2-dependent neuronal CliScience · 2024Article
- Molecular and functional profiling of cell diversity and identity in the lateral superior olive, an auditory brainstem center with ascending and descending projections.Frontiers in cellular neuroscience · 2024Article
- Spectrin-beta 2 facilitates the selective accumulation of GABACommunications biology · 2023Article
- Shisa7 phosphorylation regulates GABAergic transmission and neurodevelopmental behaviors.Neuropsychopharmacology : official publication of the American College of Neuropsychopharmacology · 2022Article
- Recruitment of Plasma Membrane GABA-A Receptors by Submembranous Gephyrin/Collybistin Clusters.Cellular and molecular neurobiology · 2022Article
- Analyzing the mechanisms that facilitate the subtype-specific assembly ofFrontiers in molecular neuroscience · 2022Article
- Regulation of GABATrends in neurosciences · 2021Review
- Phosphorylation on Ser-359 of the α2 subunit in GABA type A receptors down-regulates their density at inhibitory synapses.The Journal of biological chemistry · 2020Article
- Inhibitory synaptic transmission tuned by CaDevelopment, growth & differentiation · 2020Review
- Direct Interaction of PP2A Phosphatase with GABAThe Journal of neuroscience : the official journal of the Society for Neuroscience · 2020Article
- Isolation and Characterization of Multi-Protein Complexes Enriched in the K-Cl Co-transporter 2 From Brain Plasma Membranes.Frontiers in molecular neuroscience · 2020Article
- Essential role for InSyn1 in dystroglycan complex integrity and cognitive behaviors in mice.eLife · 2019Article
- Shisa7 is a GABAScience (New York, N.Y.) · 2019Article
- Identification of a Core Amino Acid Motif within the α Subunit of GABACell reports · 2019Article
- Multiple functional neurosteroid binding sites on GABAA receptors.PLoS biology · 2019Article
- Cellular Mechanisms Contributing to the Functional Heterogeneity of GABAergic Synapses.Frontiers in molecular neuroscience · 2019Article
- Diazepam Accelerates GABAFrontiers in cellular neuroscience · 2019Article
- Targeting GABAFrontiers in molecular neuroscience · 2019Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
Abstract
The accumulation of γ-aminobutyric acid receptors (GABAARs) at the appropriate postsynaptic sites is critical for determining the efficacy of fast inhibitory neurotransmission. Although we know that the majority of synaptic GABAAR subtypes are assembled from α1-3, β, and γ2 subunits, our understanding of how neurons facilitate their targeting to and stabilization at inhibitory synapses is rudimentary. To address these issues, we have created knock-in mice in which the pH-sensitive green fluorescent protein (GFP) and the Myc epitope were introduced to the extracellular domain of the mature receptor α2 subunit (pHα2). Using immunoaffinity purification and mass spectroscopy, we identified a stable complex of 174 proteins that were associated with pHα2, including other GABAAR subunits, and previously identified receptor-associated proteins such as gephyrin and collybistin. 149 of these proteins were novel GABAAR binding partners and included G-protein-coupled receptors and ion channel subunits, proteins that regulate trafficking and degradation, regulators of protein phosphorylation, GTPases, and a number of proteins that regulate their activity. Notably, members of the postsynaptic density family of proteins that are critical components of excitatory synapses were not associated with GABAARs. Crucially, we demonstrated for a subset of these novel proteins (including cullin1, ephexin, potassium channel tetramerization domain containing protein 12, mitofusin2, metabotropic glutamate receptor 5, p21-activated kinase 7, and Ras-related protein 5A) bind directly to the intracellular domains of GABAARs, validating our proteomic analysis. Thus, our experiments illustrate the complexity of the GABAAR proteome and enhance our understanding of the mechanisms neurons use to construct inhibitory synapses.
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