ArticleThe Journal of biological chemistry2008
A conserved Cys-loop receptor aspartate residue in the M3-M4 cytoplasmic loop is required for GABAA receptor assembly.
Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 43 citations in OpenAlex.
- Intracellular regulation of a serotonin-gated ion channel links receptor trafficking to memory.iScience · 2026Article
- Two residues determine nicotinic acetylcholine receptor requirement for RIC-3.Protein science : a publication of the Protein Society · 2023Article
- Mutations of the nACh Receptor M4 Helix Reveal Different Phenotypes in Different Expression Systems: Could Lipids be Responsible?Frontiers in physiology · 2022Article
- Deorphanization of novel biogenic amine-gated ion channels identifies a new serotonin receptor for learning.Current biology : CB · 2021Article
- AJournal of medical genetics · 2017Article
- Differential protein structural disturbances and suppression of assembly partners produced by nonsense GABRG2 epilepsy mutations: implications for disease phenotypic heterogeneity.Scientific reports · 2016Article
- Three epilepsy-associated GABRG2 missense mutations at the γ+/β- interface disrupt GABAA receptor assembly and trafficking by similar mechanisms but to different extents.Neurobiology of disease · 2014Article
- Co-expression of γ2 subunits hinders processing of N-linked glycans attached to the N104 glycosylation sites of GABAA receptor β2 subunits.Neurochemical research · 2014Article
- An intracellular redox sensor for reactive oxygen species at the M3-M4 linker of GABAA ρ1 receptors.British journal of pharmacology · 2014Article
- The minimum M3-M4 loop length of neurotransmitter-activated pentameric receptors is critical for the structural integrity of cytoplasmic portals.The Journal of biological chemistry · 2013Article
- Altered cortical GABAA receptor composition, physiology, and endocytosis in a mouse model of a human genetic absence epilepsy syndrome.The Journal of biological chemistry · 2013Article
- Impaired surface αβγ GABA(A) receptor expression in familial epilepsy due to a GABRG2 frameshift mutation.Neurobiology of disease · 2013Article
- The GABRG2 nonsense mutation, Q40X, associated with Dravet syndrome activated NMD and generated a truncated subunit that was partially rescued by aminoglycoside-induced stop codon read-through.Neurobiology of disease · 2012Article
- Article
- The GABRA6 mutation, R46W, associated with childhood absence epilepsy, alters 6β22 and 6β2 GABA(A) receptor channel gating and expression.The Journal of physiology · 2011Article
- Homeostatic strengthening of inhibitory synapses is mediated by the accumulation of GABA(A) receptors.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2011Article
- Discrete M3-M4 intracellular loop subdomains control specific aspects of γ-aminobutyric acid type A receptor function.The Journal of biological chemistry · 2011Article
- The effect of HSP-causing mutations in SPG3A and NIPA1 on the assembly, trafficking, and interaction between atlastin-1 and NIPA1.Molecular and cellular neurosciences · 2011Article
- Slow degradation and aggregation in vitro of mutant GABAA receptor gamma2(Q351X) subunits associated with epilepsy.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2010Article
- Glycosylation of {beta}2 subunits regulates GABAA receptor biogenesis and channel gating.The Journal of biological chemistry · 2010Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Members of the Cys-loop superfamily of ligand-gated ion channels, which mediate fast synaptic transmission in the nervous system, are assembled as heteropentamers from a large repertoire of neuronal subunits. Although several motifs in subunit N-terminal domains are known to be important for subunit assembly, increasing evidence points toward a role for C-terminal domains. Using a combination of flow cytometry, patch clamp recording, endoglycosidase H digestion, brefeldin A treatment, and analytic centrifugation, we identified a highly conserved aspartate residue at the boundary of the M3-M4 loop and the M4 domain that was required for binary and ternary gamma-aminobutyric acid type A receptor surface expression. Mutation of this residue caused mutant and partnering subunits to be retained in the endoplasmic reticulum, reflecting impaired forward trafficking. Interestingly although mutant and partnering wild type subunits could be coimmunoprecipitated, analytic centrifugation studies demonstrated decreased formation of pentameric receptors, suggesting that this residue played an important role in later steps of subunit oligomerization. We thus conclude that C-terminal motifs are also important determinants of Cys-loop receptor assembly.
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