ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2001
The C-terminal domains of the GABA(b) receptor subunits mediate intracellular trafficking but are not required for receptor signaling.
Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
61 citing papers in PubMed, 159 citations in OpenAlex.
- Human-specific multicopy gene FRMPD2 promotes synapse formation via recruitment of neuroligin 1.bioRxiv : the preprint server for biology · 2026Article
- Functional and structural basis of a negative allostery within GABANature communications · 2026Article
- Structural Basis of GABAAdvanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Presynaptic hyperexcitability reversed by positive allosteric modulation of a GABABR epilepsy variant.Brain : a journal of neurology · 2025Article
- The Critical Role of the Shroom Family Proteins in Morphogenesis, Organogenesis and Disease.Phenomics (Cham, Switzerland) · 2024Review
- A Bright Future? A Perspective on Class C GPCR Based Genetically Encoded Biosensors.ACS chemical neuroscience · 2024Review
- Mechanisms and Regulation of Neuronal GABACurrent topics in behavioral neurosciences · 2022Review
- Ectopic activation of GABANature ecology & evolution · 2021Article
- Extramembranous Regions in G Protein-Coupled Receptors: Cinderella in Receptor Biology?The Journal of membrane biology · 2019Review
- Rearrangement of the transmembrane domain interfaces associated with the activation of a GPCR hetero-oligomer.Nature communications · 2019Article
- Structural biology of GABANeuropharmacology · 2018Review
- GABABMC cancer · 2018Article
- Epilepsy and intellectual disability linked protein Shrm4 interaction with GABANature communications · 2017Article
- Cloning of the GABAFrontiers in neuroanatomy · 2016Article
- Controlling NMDA receptor subunit composition using ectopic retention signals.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2014Article
- Glutamine synthetase stability and subcellular distribution in astrocytes are regulated by γ-aminobutyric type B receptors.The Journal of biological chemistry · 2014Article
- GABAB receptor phosphorylation regulates KCTD12-induced K⁺ current desensitization.Biochemical pharmacology · 2014Article
- Chaperoning G protein-coupled receptors: from cell biology to therapeutics.Endocrine reviews · 2014Review
- Transport along the dendritic endoplasmic reticulum mediates the trafficking of GABAB receptors.Journal of cell science · 2014Article
- Heterodimeric coiled-coil interactions of human GABAB receptor.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
1 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
13 authors at 3 institutions in 2 countries.
Funding
Abstract
GABA(B) receptors are G-protein-coupled receptors that mediate slow synaptic inhibition in the brain and spinal cord. These receptors are heterodimers assembled from GABA(B1) and GABA(B2) subunits, neither of which is capable of producing functional GABA(B) receptors on homomeric expression. GABA(B1,) although able to bind GABA, is retained within the endoplasmic reticulum (ER) when expressed alone. In contrast, GABA(B2) is able to access the cell surface when expressed alone but does not couple efficiently to the appropriate effector systems or produce any detectable GABA-binding sites. In the present study, we have constructed chimeric and truncated GABA(B1) and GABA(B2) subunits to explore further GABA(B) receptor signaling and assembly. Removal of the entire C-terminal intracellular domain of GABA(B1) results in plasma membrane expression without the production of a functional GABA(B) receptor. However, coexpression of this truncated GABA(B1) subunit with either GABA(B2) or a truncated GABA(B2) subunit in which the C terminal has also been removed is capable of functional signaling via G-proteins. In contrast, transferring the entire C-terminal tail of GABA(B1) to GABA(B2) leads to the ER retention of the GABA(B2) subunit when expressed alone. These results indicate that the C terminal of GABA(B1) mediates the ER retention of this protein and that neither of the C-terminal tails of GABA(B1) or GABA(B2) is an absolute requirement for functional coupling of heteromeric receptors. Furthermore although GABA(B1) is capable of producing GABA-binding sites, GABA(B2) is of central importance in the functional coupling of heteromeric GABA(B) receptors to G-proteins and the subsequent activation of effector systems.
Indexed as
Identifiers
11160390PMC6762247W2157194745What OpenQuestion holds
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.