ArticleThe Journal of biological chemistry2010
Glycosylation of {beta}2 subunits regulates GABAA receptor biogenesis and channel gating.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 40 citations in OpenAlex.
- A pore-facing glycan constrains GABACommunications biology · 2026Article
- Direct modulation of human GABA-A αFrontiers in neuroscience · 2026Review
- Glycosylation disorders in pediatric epilepsy: pathophysiology, imaging and precision therapy.Frontiers in neurology · 2026Review
- Improving Proteostasis of Trafficking-Deficient GABAACS chemical neuroscience · 2025Article
- A Pore-Facing Glycan Determines GABAA Receptor Subunit Stoichiometry and Gating Behavior.Research square · 2025Article
- Aberrant glycosylation in schizophrenia: insights into pathophysiological mechanisms and therapeutic potentials.Frontiers in pharmacology · 2024Review
- Known and Unexplored Post-Translational Modification Pathways in Schizophrenia.Advances in experimental medicine and biology · 2022Article
- Glycosylation and its implications in breast cancer.Expert review of proteomics · 2019Review
- Expression and purification of a functional heteromeric GABAA receptor for structural studies.PloS one · 2018Article
- N-glycan content modulates kainate receptor functional properties.The Journal of physiology · 2017Article
- Epileptic encephalopathy de novo GABRB mutations impair γ-aminobutyric acid type A receptor function.Annals of neurology · 2016Article
- Article
- Abnormal subcellular localization of GABAA receptor subunits in schizophrenia brain.Translational psychiatry · 2015Article
- Neuronal gamma-aminobutyric acid (GABA) type A receptors undergo cognate ligand chaperoning in the endoplasmic reticulum by endogenous GABA.Frontiers in cellular neuroscience · 2015Article
- A nationwide survey of PMM2-CDG in Italy: high frequency of a mild neurological variant associated with the L32R mutation.Journal of neurology · 2015Article
- Crystal structure of a human GABAA receptor.Nature · 2014Article
- 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
- Modulation of ionotropic glutamate receptor function by vertebrate galectins.The Journal of physiology · 2014Article
- N-Glycosylation of GABAA receptor subunits is altered in Schizophrenia.Neuropsychopharmacology : official publication of the American College of Neuropsychopharmacology · 2014Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 3 countries.
Funding
Abstract
γ-aminobutyric acid type A (GABA(A)) receptors are heteropentameric glycoproteins. Based on consensus sequences, the GABA(A) receptor β2 subunit contains three potential N-linked glycosylation sites, Asn-32, Asn-104, and Asn-173. Homology modeling indicates that Asn-32 and Asn-104 are located before the α1 helix and in loop L3, respectively, near the top of the subunit-subunit interface on the minus side, and that Asn-173 is located in the Cys-loop near the bottom of the subunit N-terminal domain. Using site-directed mutagenesis, we demonstrated that all predicted β2 subunit glycosylation sites were glycosylated in transfected HEK293T cells. Glycosylation of each site, however, produced specific changes in α1β2 receptor surface expression and function. Although glycosylation of Asn-173 in the Cys-loop was important for stability of β2 subunits when expressed alone, results obtained with flow cytometry, brefeldin A treatment, and endo-β-N-acetylglucosaminidase H digestion suggested that glycosylation of Asn-104 was required for efficient α1β2 receptor assembly and/or stability in the endoplasmic reticulum. Patch clamp recording revealed that mutation of each site to prevent glycosylation decreased peak α1β2 receptor current amplitudes and altered the gating properties of α1β2 receptor channels by reducing mean open time due to a reduction in the proportion of long open states. In addition to functional heterogeneity, endo-β-N-acetylglucosaminidase H digestion and glycomic profiling revealed that surface β2 subunit N-glycans at Asn-173 were high mannose forms that were different from those of Asn-32 and N104. Using a homology model of the pentameric extracellular domain of α1β2 channel, we propose mechanisms for regulation of GABA(A) receptors by glycosylation.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.