ArticleThe Journal of biological chemistry2011
Gamma-aminobutyric acid type B (GABA(B)) receptor internalization is regulated by the R2 subunit.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 30 citations in OpenAlex.
- GPCR Heterodimers: Implications for Biased Signaling.Handbook of experimental pharmacology · 2026Review
- Presynaptic hyperexcitability reversed by positive allosteric modulation of a GABABR epilepsy variant.Brain : a journal of neurology · 2025Article
- Impact of aging on the GABAbioRxiv : the preprint server for biology · 2024Article
- CGP7930 - An allosteric modulator of GABANeuropharmacology · 2023Article
- Cross-modal reaction of auditory and visual cortices after long-term bilateral hearing deprivation in the rat.Brain structure & function · 2020Article
- CaMolecular neurobiology · 2019Article
- Genome-scale identification of cellular pathways required for cell surface recognition.Genome research · 2018Article
- Neuronal Chloride Regulation via KCC2 Is Modulated through a GABAThe Journal of neuroscience : the official journal of the Society for Neuroscience · 2017Article
- Epilepsy and intellectual disability linked protein Shrm4 interaction with GABANature communications · 2017Article
- Lys-63-linked Ubiquitination of γ-Aminobutyric Acid (GABA), Type B1, at Multiple Sites by the E3 Ligase Mind Bomb-2 Targets GABAB Receptors to Lysosomal Degradation.The Journal of biological chemistry · 2016Article
- Phospho-dependent Accumulation of GABABRs at Presynaptic Terminals after NMDAR Activation.Cell reports · 2016Article
- Snake neurotoxin α-bungarotoxin is an antagonist at native GABA(A) receptors.Neuropharmacology · 2015Article
- A naturally occurring GIP receptor variant undergoes enhanced agonist-induced desensitization, which impairs GIP control of adipose insulin sensitivity.Molecular and cellular biology · 2014Article
- Using an α-bungarotoxin binding site tag to study GABA A receptor membrane localization and trafficking.Journal of visualized experiments : JoVE · 2014Article
- Article
- Neuronal phenotype dependency of agonist-induced internalization of the 5-HT(1A) serotonin receptor.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2014Article
- The Concise Guide to PHARMACOLOGY 2013/14: G protein-coupled receptors.British journal of pharmacology · 2013Article
- Up-regulation of GABA(B) receptor signaling by constitutive assembly with the K+ channel tetramerization domain-containing protein 12 (KCTD12).The Journal of biological chemistry · 2013Article
- Mutations in AP2S1 cause familial hypocalciuric hypercalcemia type 3.Nature genetics · 2013Article
- Sushi domains confer distinct trafficking profiles on GABAB receptors.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
γ-Aminobutyric acid type B (GABA(B)) receptors are important for slow synaptic inhibition in the CNS. The efficacy of inhibition is directly related to the stability of cell surface receptors. For GABA(B) receptors, heterodimerization between R1 and R2 subunits is critical for cell surface expression and signaling, but how this determines the rate and extent of receptor internalization is unknown. Here, we insert a high affinity α-bungarotoxin binding site into the N terminus of the R2 subunit and reveal its dominant role in regulating the internalization of GABA(B) receptors in live cells. To simultaneously study R1a and R2 trafficking, a new α-bungarotoxin binding site-labeling technique was used, allowing α-bungarotoxin conjugated to different fluorophores to selectively label R1a and R2 subunits. This approach demonstrated that R1a and R2 are internalized as dimers. In heterologous expression systems and neurons, the rates and extents of internalization for R1aR2 heteromers and R2 homomers are similar, suggesting a regulatory role for R2 in determining cell surface receptor stability. The fast internalization rate of R1a, which has been engineered to exit the endoplasmic reticulum, was slowed to that of R2 by truncating the R1a C-terminal tail or by removing a dileucine motif in its coiled-coil domain. Slowing the rate of internalization by co-assembly with R2 represents a novel role for GPCR heterodimerization whereby R2 subunits, via their C terminus coiled-coil domain, mask a dileucine motif on R1a subunits to determine the surface stability of the GABA(B) receptor.
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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.