ArticleThe EMBO journal2007
Identification of the PIP2-binding site on Kir6.2 by molecular modelling and functional analysis.
Article in The EMBO journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.
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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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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.
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Who cites it
53 citing papers in PubMed, 81 citations in OpenAlex.
- Molecular Dynamics Simulation of Kir6.2 Variants Reveals Potential Association with Diabetes Mellitus.Molecules (Basel, Switzerland) · 2024Article
- Expression and Purification of Glycosyltransferase DnmS fromMicroorganisms · 2023Article
- From Crosstalk to Synergism: The Combined Effect of Cholesterol and PI(4,5)PAdvances in experimental medicine and biology · 2023Review
- The dynamic interplay of PIPThe Journal of physiology · 2022Article
- Structural insights into the mechanism of pancreatic KNature communications · 2022Article
- In silico investigation of Alsin RLD conformational dynamics and phosphoinositides binding mechanism.PloS one · 2022Article
- Expression of truncated Kir6.2 promotes insertion of functionally inverted ATP-sensitive KScientific reports · 2021Article
- From Bench to Biomolecular Simulation: Phospholipid Modulation of Potassium Channels.Journal of molecular biology · 2021Review
- Simulating PIPFrontiers in molecular biosciences · 2021Article
- Striking a balance: PIPExploration of neuroprotective therapy · 2021Article
- Evaluating inositol phospholipid interactions with inward rectifier potassium channels and characterising their role in disease.Communications chemistry · 2020Article
- Structure-based enzyme engineering improves donor-substrate recognition of Arabidopsis thaliana glycosyltransferases.The Biochemical journal · 2020Article
- New insights into KNature reviews. Endocrinology · 2020Review
- A Self-Assembling Lipidic Peptide and Selective Partial V2 Receptor Agonist Inhibits Urine Production.Scientific reports · 2020Article
- Characterization of Lipid-Protein Interactions and Lipid-Mediated Modulation of Membrane Protein Function through Molecular Simulation.Chemical reviews · 2019Review
- Protein arginine methylation facilitates KCNQ channel-PIP2 interaction leading to seizure suppression.eLife · 2016Article
- KATP Channels in the Cardiovascular System.Physiological reviews · 2016Review
- Functional and Modeling Studies of the Transmembrane Region of the TRPM8 Channel.Biophysical journal · 2015Article
- A Conserved Residue Cluster That Governs Kinetics of ATP-dependent Gating of Kir6.2 Potassium Channels.The Journal of biological chemistry · 2015Article
- Identification of the Conformational transition pathway in PIP2 Opening Kir Channels.Scientific reports · 2015Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
ATP-sensitive potassium (K(ATP)) channels couple cell metabolism to electrical activity by regulating K(+) fluxes across the plasma membrane. Channel closure is facilitated by ATP, which binds to the pore-forming subunit (Kir6.2). Conversely, channel opening is potentiated by phosphoinositol bisphosphate (PIP(2)), which binds to Kir6.2 and reduces channel inhibition by ATP. Here, we use homology modelling and ligand docking to identify the PIP(2)-binding site on Kir6.2. The model is consistent with a large amount of functional data and was further tested by mutagenesis. The fatty acyl tails of PIP(2) lie within the membrane and the head group extends downwards to interact with residues in the N terminus (K39, N41, R54), transmembrane domains (K67) and C terminus (R176, R177, E179, R301) of Kir6.2. Our model suggests how PIP(2) increases channel opening and decreases ATP binding and channel inhibition. It is likely to be applicable to the PIP(2)-binding site of other Kir channels, as the residues identified are conserved and influence PIP(2) sensitivity in other Kir channel family members.
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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.