Regular ArticleAnalysis of GABAA Receptor Assembly in Mammalian Cell Lines and Hippocampal Neurons Using γ2 Subunit Green Fluorescent Protein Chimeras
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2023, Progress in Molecular Biology and Translational ScienceFlumazenil decreases surface expression of α4β2δ GABA<inf>A</inf> receptors by increasing the rate of receptor internalization
2016, Brain Research BulletinCitation Excerpt :However, concomitant 48 h treatment with flumazenil partially reversed the effect of GABA plus THP treatment, increasing intracellular expression by ∼50% compared to GABA plus THP (P < 0.05), suggesting that it may have an effect on receptor trafficking or receptor re-cycling as detailed in the discussion. Internalization via the clathrin-coated pit has been considered the primary mechanism for reducing GABAAR surface expression at synaptic (Kittler et al., 2000) and extrasynaptic sites (Joshi and Kapur, 2009), but this mechanism has not yet been investigated in α4β2δ receptor down-regulation. To test if this same mechanism is responsible for down-regulation of extrasynaptic α4β2δ membrane receptors by flumazenil we used dynasore (80 μM) to block internalization through dynamin inhibition in HEK-293 cells.
Ring finger protein 34 (RNF34) interacts with and promotes γ-aminobutyric acid type-a receptor degradation via ubiquitination of the γ2 subunit
2014, Journal of Biological ChemistryCitation Excerpt :Other reports using bacterially expressed E3 UBL for in vitro ubiquitinating synaptic proteins also show low activity, and only a very small fraction of the synaptic substrates become ubiquitinated (14, 51). Previous studies by us and others have shown that α, β, and γ2 subunits could assemble into functional GABAARs and target to the cell membrane when they were co-expressed in HEK293 cells (38, 54–57). Our data indicate that RNF34 reduces the protein expression level of the γ2 subunit, regardless of whether γ2 is expressed alone or expressed together with α1 and β3 subunits forming assembled α1β3γ2 pentameric GABAARs at the cell surface.
Molecular Motor KIF5A Is Essential for GABA<inf>A</inf> Receptor Transport, and KIF5A Deletion Causes Epilepsy
2012, NeuronCitation Excerpt :After washout of BFA, cells were fixed and incubated with an anti-GFP antibody without permeabilization. Because the GFP tag of the GABAAR-GFP construct is located at the outer surface after membrane insertion (Kittler et al., 2000), we could detect the surface receptor using this procedure. As a result, we observed a significant delay in surface expression of GABAAR-GFP in Kif5a-KO neurons (Figures 8B and 8E).