ArticleThe Journal of biological chemistry2012
Structural basis for modulation of gating property of G protein-gated inwardly rectifying potassium ion channel (GIRK) by i/o-family G protein α subunit (Gαi/o).
Article in The Journal of biological chemistry, 2012. 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, 35 citations in OpenAlex.
- Live-cell quantitative monitoring reveals distinct, high-affinity Gβγ regulations of GIRK2 and GIRK1/2 channels.Nature communications · 2025Article
- Live-cell quantitative monitoring reveals distinct, high-affinity Gβγ regulations of GIRK2 and GIRK1/2 channels.bioRxiv : the preprint server for biology · 2025Article
- The structural basis of the G protein-coupled receptor and ion channel axis.Current research in structural biology · 2025Review
- Neuronal G protein-gated KAmerican journal of physiology. Cell physiology · 2022Review
- The Conformational Dynamics of Heterotrimeric G Proteins During GPCR-Mediated Activation.Sub-cellular biochemistry · 2022Review
- Function-Related Dynamics in Multi-Spanning Helical Membrane Proteins Revealed by Solution NMR.Membranes · 2021Review
- The small molecule GAT1508 activates brain-specific GIRK1/2 channel heteromers and facilitates conditioned fear extinction in rodents.The Journal of biological chemistry · 2020Article
- Structural mechanism underlying G protein family-specific regulation of G protein-gated inwardly rectifying potassium channel.Nature communications · 2019Article
- Domain insertion permissibility-guided engineering of allostery in ion channels.Nature communications · 2019Article
- Structural basis for the ethanol action on G-protein-activated inwardly rectifying potassium channel 1 revealed by NMR spectroscopy.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Gi/o-coupled muscarinic receptors co-localize with GIRK channel for efficient channel activation.PloS one · 2018Article
- Dynamic regulation of GDP binding to G proteins revealed by magnetic field-dependent NMR relaxation analyses.Nature communications · 2017Article
- Structural basis of control of inward rectifier Kir2 channel gating by bulk anionic phospholipids.The Journal of general physiology · 2016Article
- A Quantitative Model of the GIRK1/2 Channel Reveals That Its Basal and Evoked Activities Are Controlled by Unequal Stoichiometry of Gα and Gβγ.PLoS computational biology · 2015Article
- Recruitment of Gβγ controls the basal activity of G-protein coupled inwardly rectifying potassium (GIRK) channels: crucial role of distal C terminus of GIRK1.The Journal of physiology · 2014Article
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- A mechanism regulating G protein-coupled receptor signaling that requires cycles of protein palmitoylation and depalmitoylation.The Journal of biological chemistry · 2014Article
- New insights into the therapeutic potential of Girk channels.Trends in neurosciences · 2014Review
- Kir3 channel signaling complexes: focus on opioid receptor signaling.Frontiers in cellular neuroscience · 2014Review
- Alcohol modulation of G-protein-gated inwardly rectifying potassium channels: from binding to therapeutics.Frontiers in physiology · 2014Review
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
G protein-gated inwardly rectifying potassium channel (GIRK) plays a crucial role in regulating heart rate and neuronal excitability. The gating of GIRK is regulated by the association and dissociation of G protein βγ subunits (Gβγ), which are released from pertussis toxin-sensitive G protein α subunit (Gα(i/o)) upon GPCR activation in vivo. Several lines of evidence indicate that Gα(i/o) also interacts directly with GIRK, playing functional roles in the signaling efficiency and the modulation of the channel activity. However, the underlying mechanism for GIRK regulation by Gα(i/o) remains to be elucidated. Here, we performed NMR analyses of the interaction between the cytoplasmic region of GIRK1 and Gα(i3) in the GTP-bound state. The NMR spectral changes of Gα upon the addition of GIRK as well as the transferred cross-saturation (TCS) results indicated their direct binding mode, where the K(d) value was estimated as ∼1 mm. The TCS experiments identified the direct binding sites on Gα and GIRK as the α2/α3 helices on the GTPase domain of Gα and the αA helix of GIRK. In addition, the TCS and paramagnetic relaxation enhancement results suggested that the helical domain of Gα transiently interacts with the αA helix of GIRK. Based on these results, we built a docking model of Gα and GIRK, suggesting the molecular basis for efficient GIRK deactivation by Gα(i/o).
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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.