ArticleNature communications2019
Structural mechanism underlying G protein family-specific regulation of G protein-gated inwardly rectifying potassium channel.
Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 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
32 citing papers in PubMed, 55 citations in OpenAlex.
- A critical residue mediates proper assembly and gating of GIRK2 channels.The Journal of general physiology · 2026Article
- Genetic loci responsible for atrioventricular block in children.Frontiers in cell and developmental biology · 2026Review
- Direct crosstalk between GPCRs and ion channels via G proteins.Experimental & molecular medicine · 2025Review
- Harnessing biomaterials for tuning inflammation: A neutrophil-centric perspective.Materials today. Bio · 2025Review
- Live-cell quantitative monitoring reveals distinct, high-affinity Gβγ regulations of GIRK2 and GIRK1/2 channels.Nature communications · 2025Article
- Gene Expression Associated With Behaviour Manipulation in Wood Ants Infected With Larval Lancet Fluke, Dicrocoelium dendriticum.Molecular ecology · 2025Article
- The structural basis of the G protein-coupled receptor and ion channel axis.Current research in structural biology · 2025Review
- Cannabinoid Modulation of Excitability and Short-Term Neuronal Dynamics in the Dorsal and Ventral Hippocampus.Biology · 2025Article
- Deciphering complexity of GPCR signaling and modulation: implications and perspectives for drug discovery.Clinical science (London, England : 1979) · 2025Review
- Article
- Pre-existing parasympathetic dominance seems to cause persistent heart rate slowing after 6 months of fingolimod treatment in patients with multiple sclerosis.Clinical autonomic research : official journal of the Clinical Autonomic Research Society · 2025Article
- Identification of Potential Modulators of a Pathogenic G Protein-Gated Inwardly Rectifying KMolecules (Basel, Switzerland) · 2023Article
- Shared Mechanisms of GABAergic and Opioidergic Transmission Regulate Corticolimbic Reward Systems and Cognitive Aspects of Motivational Behaviors.Brain sciences · 2023Review
- Molecular architecture of the GαNature communications · 2023Article
- A visual opsin from jellyfish enables precise temporal control of G protein signalling.Nature communications · 2023Article
- Mapping the conformational landscape of the stimulatory heterotrimeric G protein.Nature structural & molecular biology · 2023Article
- The unique structural characteristics of the Kir 7.1 inward rectifier potassium channel: a novel player in energy homeostasis control.American journal of physiology. Cell physiology · 2023Review
- Histaminergic regulation of food intake.Frontiers in endocrinology · 2023Review
- Natural Sympathomimetic Drugs: From Pharmacology to Toxicology.Biomolecules · 2022Review
- The Relevance of GIRK Channels in Heart Function.Membranes · 2022Review
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
G protein-gated inwardly rectifying potassium channel (GIRK) plays a key role in regulating neurotransmission. GIRK is opened by the direct binding of the G protein βγ subunit (Gβγ), which is released from the heterotrimeric G protein (Gαβγ) upon the activation of G protein-coupled receptors (GPCRs). GIRK contributes to precise cellular responses by specifically and efficiently responding to the Gi/o-coupled GPCRs. However, the detailed mechanisms underlying this family-specific and efficient activation are largely unknown. Here, we investigate the structural mechanism underlying the Gi/o family-specific activation of GIRK, by combining cell-based BRET experiments and NMR analyses in a reconstituted membrane environment. We show that the interaction formed by the αA helix of Gαi/o mediates the formation of the Gαi/oβγ-GIRK complex, which is responsible for the family-specific activation of GIRK. We also present a model structure of the Gαi/oβγ-GIRK complex, which provides the molecular basis underlying the specific and efficient regulation of GIRK.
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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.