ArticleThe EMBO journal2001
Allosteric interactions between GB1 and GB2 subunits are required for optimal GABA(B) receptor function.
Article in The EMBO journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 123 papers.
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Who cites it
123 citing papers in PubMed, 364 citations in OpenAlex.
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- Smooth operator(s): dialing up and down neurotransmitter responses by G-protein regulators.Trends in cell biology · 2025Review
- An Alternative Mode of GPCR Transactivation: Activation of GPCRs by Adhesion GPCRs.International journal of molecular sciences · 2025Review
- Structural insights into the regulation of monomeric and dimeric apelin receptor.Nature communications · 2025Article
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- Transgenic line for characterizing GABA-receptor expression to study the neural basis of olfaction in the yellow-fever mosquito.Frontiers in physiology · 2024Article
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- Disrupting GPCR Complexes with Smart Drug-like Peptides.Pharmaceutics · 2022Review
- Structural Basis of GABACurrent topics in behavioral neurosciences · 2022Review
- Emerging Role of Neuron-Glia in Neurological Disorders: At a Glance.Oxidative medicine and cellular longevity · 2022Review
- GPCR heteromers: An overview of their classification, function and physiological relevance.Frontiers in endocrinology · 2022Review
- Class A and C GPCR Dimers in Neurodegenerative Diseases.Current neuropharmacology · 2022Review
- GABACurrent topics in behavioral neurosciences · 2022Review
- Mechanisms and Regulation of Neuronal GABACurrent topics in behavioral neurosciences · 2022Review
- GABACurrent topics in behavioral neurosciences · 2022Article
- G-protein coupled receptors and synaptic plasticity in sleep deprivation.World journal of psychiatry · 2021Review
- A nanobody activating metabotropic glutamate receptor 4 discriminates between homo- and heterodimers.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
63 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Recent studies on G-protein-coupled receptors revealed that they can dimerize. However, the role of each subunit in the activation process remains unclear. The gamma-amino-n-butyric acid type B (GABA(B)) receptor is comprised of two subunits: GB1 and GB2. Both consist of an extracellular domain (ECD) and a heptahelical domain composed of seven transmembrane alpha-helices, loops and the C-terminus (HD). Whereas GB1 ECD plays a critical role in ligand binding, GB2 is required not only to target GB1 subunit to the cell surface but also for receptor activation. Here, by analysing chimeric GB subunits, we show that only GB2 HD contains the determinants required for G-protein signalling. However, the HD of GB1 improves coupling efficacy. Conversely, although GB1 ECD is sufficient to bind GABA(B) ligands, the ECD of GB2 increases the agonist affinity on GB1, and is necessary for agonist activation of the receptor. These data indicate that multiple allosteric interactions between the two subunits are required for wild-type functioning of the GABA(B) receptor and highlight further the importance of the dimerization process in GPCR activation.
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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.