ArticleProceedings of the National Academy of Sciences of the United States of America2014
Heterodimeric coiled-coil interactions of human GABAB receptor.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
What it found
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Who cites it
26 citing papers in PubMed, 54 citations in OpenAlex.
- Clinical and Molecular Genetic Characterization of Landau Kleffner Syndrome: An Observational Cohort and Experimental Study.Annals of neurology · 2025Observational
- Structural Basis of GABAAdvanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Article
- Impact of aging on the GABAbioRxiv : the preprint server for biology · 2024Article
- Selective Cell-Surface Expression of Triheteromeric NMDA Receptors.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Cholesterol in Class C GPCRs: Role, Relevance, and Localization.Membranes · 2023Article
- Differential effects of mutations of POPDC proteins on heteromeric interaction and membrane trafficking.Acta neuropathologica communications · 2023Article
- Filamin A organizes γ‑aminobutyric acid type B receptors at the plasma membrane.Nature communications · 2023Article
- Oligomerization of the heteromeric γ-aminobutyric acid receptor GABAScientific reports · 2022Article
- Membrane-mediated protein interactions drive membrane protein organization.Nature communications · 2022Article
- Mechanisms and Regulation of Neuronal GABACurrent topics in behavioral neurosciences · 2022Review
- Structural Basis of GABACurrent topics in behavioral neurosciences · 2022Review
- Molecular mechanisms of metabotropic GABAScience advances · 2021Review
- Single-Molecule Fluorescence Imaging Reveals GABAB Receptor Aggregation State Changes.Frontiers in chemistry · 2021Article
- Structure of human GABANature · 2020Article
- The GABAMolecules (Basel, Switzerland) · 2020Review
- Direct Interaction of PP2A Phosphatase with GABAThe Journal of neuroscience : the official journal of the Society for Neuroscience · 2020Article
- Multi-functionality of proteins involved in GPCR and G protein signaling: making sense of structure-function continuum with intrinsic disorder-based proteoforms.Cellular and molecular life sciences : CMLS · 2019Review
- Using the novel HiBiT tag to label cell surface relaxin receptors for BRET proximity analysis.Pharmacology research & perspectives · 2019Article
- Rearrangement of the transmembrane domain interfaces associated with the activation of a GPCR hetero-oligomer.Nature communications · 2019Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Metabotropic GABAB receptor is a G protein-coupled receptor that mediates inhibitory neurotransmission in the CNS. It functions as an obligatory heterodimer of GABAB receptor 1 (GBR1) and GABAB receptor 2 (GBR2) subunits. The association between GBR1 and GBR2 masks an endoplasmic reticulum (ER) retention signal in the cytoplasmic region of GBR1 and facilitates cell surface expression of both subunits. Here, we present, to our knowledge, the first crystal structure of an intracellular coiled-coil heterodimer of human GABAB receptor. We found that polar interactions buried within the hydrophobic core determine the specificity of heterodimer pairing. Disruption of the hydrophobic coiled-coil interface with single mutations in either subunit impairs surface expression of GBR1, confirming that the coiled-coil interaction is required to inactivate the adjacent ER retention signal of GBR1. The coiled-coil assembly buries an internalization motif of GBR1 at the heterodimer interface. The ER retention signal of GBR1 is not part of the core coiled-coil structure, suggesting that it is sterically shielded by GBR2 upon heterodimer formation.
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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.