Neuron
ArticleTwo novel GABAA receptor subunits exist in distinct neuronal subpopulations
References (36)
- et al.
A technique for radiolabeling DNA restriction endonuclease fragments to high specific activity
Anal. Biochem.
(1983) - et al.
Regulation of receptor function by protein phosphorylation
Trends Neurosci.
(1987) - et al.
High-affinity GABA receptors: autoradiographic localization
Brain Res.
(1981) - et al.
In situ hybridization for the study of gene expression in the brain
Meth. Enzymol.
(1986) The mRNAs encoding GABAA/benzodiazepine receptor subunits are localized in different cell populations of the bovine cerebellum
Neuron
(1988)- et al.
Functional chloride channels by mammalian cell expression of rat glycine receptor subunit
Neuron
(1989) - et al.
Production of single-stranded plasmid DNA
Meth. Enzymol.
(1987) - et al.
Distinct GABAA receptor a subunit mRNAs show differential patterns of expression in bovine brain
Neuron
(1988) - et al.
Patch-clamp study of γ-aminobutyric acid receptor Cl− channels in cultured astrocytes
- et al.
High efficiency transformation of mammalian cells by plasmid DNA
Mol. Cell. Biol.
(1987)
Localization of the GABAA receptor in the rat brain with a monoclonal antibody to the 57000 Mr peptide of the GABAA receptor/benzodiazepine/Cl− channel complex
J. Neurosci.
Construction and characterization of an active factor III variant lacking the central one-third of the molecule
Biochemistry
The Cerebellum as a Neuronal Machine
The strychnine-binding subunit of the glycine receptor shows homology with nicotinic acetylcholine receptors
Nature
Improved patch-clamp techniques for high resolution current recording from cells and cell-free membrane patches
Pflüger's Arch. Ges. Physiol.
The Thalamus
Structural and functional basis for GABAA receptor heterogeneity
Nature
Efficient in vitro synthesis of biologically active RNA and RNA hybridization probes from plasmids containing a bacteriophage SP6 promoter
Nucl. Acids Res.
Cited by (505)
Multiple actions of fenamates and other nonsteroidal anti-inflammatory drugs on GABA<inf>A</inf> receptors
2019, European Journal of PharmacologyCell surface expression of homomeric GABA<inf>A</inf> receptors depends on single residues in subunit transmembrane domains
2018, Journal of Biological ChemistryCitation Excerpt :A single residue exchange enabled the formation of functional α and γ2L channels without the need for auxiliary subunit co-assembly. This contrasts with WT α1 or γ2L homomers that are not expressed at the cell surface (9, 10, 36). The remarkable finding is that just single TMD residue substitutions are sufficient to bypass stringent assembly rules, preventing access to the cell surface.
To what extent is it possible to dissociate the anxiolytic and sedative/hypnotic properties of GABA<inf>A</inf> receptors modulators?
2016, Progress in Neuro-Psychopharmacology and Biological PsychiatryMethyl CpG binding protein 2 gene disruption augments tonic currents of γ-aminobutyric acid receptors in locus coeruleus neurons: Impact on neuronal excitability and breathing
2015, Journal of Biological ChemistryCitation Excerpt :However, it is still unclear how the extrasynaptic GABAARs are affected in Mecp2-null mice, which makes this study remarkable. Extrasynaptic GABAARs were first described in cerebellar cortical gray matter (37) and found later in many other brain areas, such as the cerebral cortex, dentate gyrus granule, thalamus, and neocortex (38–43). Extrasynaptic GABAARs are sensitive to low levels of ambient GABA with little desensitization.
Significance of GABA<inf>A</inf> receptor heterogeneity: Clues from developing neurons
2015, Advances in PharmacologyCitation Excerpt :In particular, bd-17 binds to an epitope common to both the β2 and β3 subunits (Ewert, Shivers, Luddens, Mohler, & Seeburg, 1990), which together account for > 80% of GABAAR (Benke, Fritschy, Trzeciak, Bannwarth, & Mohler, 1994). Strong evidence for heterogeneity nevertheless arose, in particular, from the identification of the rat δ subunit, whose distribution was shown to be largely different from the γ2 subunit, and to correspond to sites where muscimol, but not classical benzodiazepine agonists, bind with high affinity (Shivers et al., 1989). Identification of protein sequence of each of the 19 GABAAR subunits (Olsen & Sieghart, 2008) afforded the possibility to generate subunit-specific RNA probes and antibodies to investigate their relative expression patterns distribution and pharmacological properties in the adult CNS and during development.
- ‡
Present address: Pacific Biotechnology Limited, 72 Mclachlan Avenue, Rushcutters Bay 2011, Australia.