ArticleThe Journal of physiology1999
Molecular mechanism for sodium-dependent activation of G protein-gated K+ channels.
Article in The Journal of physiology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 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
50 citing papers in PubMed, 101 citations in OpenAlex.
- Mutagenesis-Centered Integrative Approaches for Identifying Binding Sites in Ion Channels and Uncovering Modulatory Mechanisms.Advances in experimental medicine and biology · 2026Review
- Molecular mechanism of GIRK2 channel gating modulated by cholesteryl hemisuccinate.Frontiers in physiology · 2024Article
- PI(4,5)PAdvances in experimental medicine and biology · 2023Article
- From Crosstalk to Synergism: The Combined Effect of Cholesterol and PI(4,5)PAdvances in experimental medicine and biology · 2023Review
- A novel small-molecule selective activator of homomeric GIRK4 channels.The Journal of biological chemistry · 2022Article
- Insight into the Phospholipid-Binding Preferences of Kir3.4.Biochemistry · 2021Article
- High-Resolution Structures of KHandbook of experimental pharmacology · 2021Article
- The small molecule GAT1508 activates brain-specific GIRK1/2 channel heteromers and facilitates conditioned fear extinction in rodents.The Journal of biological chemistry · 2020Article
- Ion Channels of the Islets in Type 2 Diabetes.Journal of molecular biology · 2020Review
- On the mechanism of GIRK2 channel gating by phosphatidylinositol bisphosphate, sodium, and the Gβγ dimer.The Journal of biological chemistry · 2019Article
- Phosphoinositides modulate the voltage dependence of two-pore channel 3.The Journal of general physiology · 2019Article
- Ivermectin and its target molecules: shared and unique modulation mechanisms of ion channels and receptors by ivermectin.The Journal of physiology · 2018Review
- Dual activation of neuronal G protein-gated inwardly rectifying potassium (GIRK) channels by cholesterol and alcohol.Scientific reports · 2017Article
- Article
- A Critical Gating Switch at a Modulatory Site in Neuronal Kir3 Channels.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2015Article
- Phosphoinositides regulate ion channels.Biochimica et biophysica acta · 2015Review
- Phosphoinositide control of membrane protein function: a frontier led by studies on ion channels.Annual review of physiology · 2015Review
- Article
- Alcohol modulation of G-protein-gated inwardly rectifying potassium channels: from binding to therapeutics.Frontiers in physiology · 2014Review
- Molecular mechanism underlying ethanol activation of G-protein-gated inwardly rectifying potassium channels.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
1. G protein-gated inwardly rectifying K+ (GIRK) channels are activated independently by Gbetagamma and internal Na+ via mechanisms requiring phosphatidylinositol phosphates. An aspartate (Asp) at position 226 in GIRK2 is crucial for Na+-dependent activation of GIRK1-GIRK2 heteromeric channels. We expressed wild-type and mutant GIRK1-GIRK2 channels in Xenopus oocytes and tested the effects of Na+ and neutralizing Asp226 on the functional interactions of the channels with phosphatidylinositol 4, 5-bisphosphate (PIP2). 2. The rate of inhibition of GIRK1-GIRK2 currents by application of anti-PIP2 antibody to inside-out membrane patches was slowed > 2-fold by the D226N mutation in GIRK2 and by increasing internal [Na+]. The reverse mutation in GIRK1 (N217D) increased the rate of inhibition. 3. The dose-response relationship for activation by purified PIP2 was shifted to lower concentrations in the presence of 20 mM Na+. 4. Three synthetic isoforms of PIP2, PI(4,5)P2, PI(3,4)P2 and PI(3,5)P2, activated GIRK channels with similar potencies. 5. We conclude that Na+ directly interacts with Asp226 of GIRK2 to reduce the negative electrostatic potential and promote the functional interaction of the channels with PIP2.
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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.