ArticleThe Journal of physiology2002
Allosteric modulation of the mouse Kir6.2 channel by intracellular H+ and ATP.
Article in The Journal of physiology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
16 citing papers in PubMed, 35 citations in OpenAlex.
- Energy substrate preference and metabolic flexibility in quiescent and oxytocin-stimulated human myometrial cells.iScience · 2026Article
- Metabolic Flexibility and Energy Substrate Utilization Regulate Contractility in the Human Myometrium.bioRxiv : the preprint server for biology · 2026Article
- Review
- Spreading depolarizations pose critical energy challenges in acute brain injury.Journal of neurochemistry · 2024Review
- Exploring the Role of Surface and Mitochondrial ATP-Sensitive Potassium Channels in Cancer: From Cellular Functions to Therapeutic Potentials.International journal of molecular sciences · 2024Review
- Stx4 is required to regulate cardiomyocyte CaHGG advances · 2022Article
- Mechanisms contributing to myocardial potassium channel diversity, regulation and remodeling.Trends in cardiovascular medicine · 2016Review
- Sensitivity of KATP channels to cellular metabolic disorders and the underlying structural basis.Acta pharmacologica Sinica · 2016Article
- Mechanisms of sudden cardiac death: oxidants and metabolism.Circulation research · 2015Review
- Muscle KATP channels: recent insights to energy sensing and myoprotection.Physiological reviews · 2010Review
- Molecular identification and functional characterization of a mitochondrial sulfonylurea receptor 2 splice variant generated by intraexonic splicing.Circulation research · 2009Article
- Protein kinase C dependent inhibition of the heteromeric Kir4.1-Kir5.1 channel.Biochimica et biophysica acta · 2007Article
- Subunit-subunit interactions are critical for proton sensitivity of ROMK: evidence in support of an intermolecular gating mechanism.Proceedings of the National Academy of Sciences of the United States of America · 2006Article
- Kir6.2 channel gating by intracellular protons: subunit stoichiometry for ligand binding and channel gating.The Journal of membrane biology · 2006Article
- Determinant role of membrane helices in K ATP channel gating.The Journal of membrane biology · 2005Article
- Functional characterization of a prokaryotic Kir channel.The Journal of biological chemistry · 2004Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
The ATP-sensitive K+ (K(ATP)) channels are regulated by intracellular H+ in addition to ATP, ADP, and phospholipids. Here we show evidence for the interaction of H+ with ATP in regulating a cloned K(ATP) channel, i.e. Kir6.2 expressed with and without the SUR1 subunit. Channel sensitivity to ATP decreases at acidic pH, while the pH sensitivity also drops in the presence of ATP. These effects are more evident in the presence of the SUR1 subunit. In the Kir6.2 + SUR1, the pH sensitivity is reduced by about 0.4 pH units with 100 microM ATP and 0.6 pH units with 1 mM ATP, while a decrease in pH from 7.4 to 6.8 lowers the ATP sensitivity by about fourfold. The Kir6.2 + SUR1 currents are strongly activated at pH 5.9-6.5 even in the presence of 1 mM ATP. The modulations appear to take place at His175 and Lys185 that are involved in proton and ATP sensing, respectively. Mutation of His175 completely eliminates the pH effect on the ATP sensitivity. Similarly, the K185E mutant-channel loses the ATP-dependent modulation of the pH sensitivity. Thus, allosteric modulations of the cloned K(ATP) channel by ATP and H+ are demonstrated. Such a regulation allows protons to activate directly the K(ATP) channels and release channel inhibition by intracellular ATP; the pH effect is further enhanced with a decrease in ATP concentration as seen in several pathophysiological conditions.
Indexed as
Identifiers
What 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.