ReviewFrontiers in physiology2014
Phosphoinositide regulation of inward rectifier potassium (Kir) channels.
Review in Frontiers in physiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 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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Who cites it
29 citing papers in PubMed, 42 citations in OpenAlex.
- Molecular mechanisms of Kir channel gating.Biochemical Society transactions · 2026Review
- Potassium channels in vascular smooth muscle cells.Physiological reviews · 2026Review
- Inhibition of lipolysis in visceral adipose tissue from obese mice and humans prevents impairment of endothelial Kir2.1 channels.Channels (Austin, Tex.) · 2025Article
- Cooperative Gating of a KJournal of the American Chemical Society · 2024Article
- Current advancements and future perspectives of long noncoding RNAs in lipid metabolism and signaling.Journal of advanced research · 2023Review
- Oxytocin-Modulated Ion Channel Ensemble Controls Depolarization, Integration and Burst Firing in CA2 Pyramidal Neurons.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2022Article
- Cryo-electron microscopy unveils unique structural features of the human Kir2.1 channel.Science advances · 2022Article
- Bivalent recognition of fatty acyl-CoA by a human integral membrane palmitoyltransferase.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- The versatile regulation of K2P channels by polyanionic lipids of the phosphoinositide and fatty acid metabolism.The Journal of general physiology · 2022Article
- Ion currents through Kir potassium channels are gated by anionic lipids.Nature communications · 2022Article
- Studying KcsA Channel Clustering Using Single Channel Voltage-Clamp Fluorescence Imaging.Frontiers in physiology · 2022Article
- Cell-Free Expression of Proton-Coupled Folate Transporter in the Presence of Nanodiscs.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Entropy in the Molecular Recognition of Membrane Protein-Lipid Interactions.The journal of physical chemistry letters · 2021Article
- Insight into the Phospholipid-Binding Preferences of Kir3.4.Biochemistry · 2021Article
- Vascular KProceedings of the National Academy of Sciences of the United States of America · 2021Article
- Simulating PIPFrontiers in molecular biosciences · 2021Article
- Impact of nanodisc lipid composition on cell-free expression of proton-coupled folate transporter.PloS one · 2021Article
- Defining how multiple lipid species interact with inward rectifier potassium (Kir2) channels.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Emerging Diversity in Lipid-Protein Interactions.Chemical reviews · 2019Review
- Characterization of Lipid-Protein Interactions and Lipid-Mediated Modulation of Membrane Protein Function through Molecular Simulation.Chemical reviews · 2019Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Inward rectifier potassium (Kir) channels are integral membrane proteins charged with a key role in establishing the resting membrane potential of excitable cells through selective control of the permeation of K(+) ions across cell membranes. In conjunction with secondary anionic phospholipids, members of this family are directly regulated by phosphoinositides (PIPs) in the absence of other proteins or downstream signaling pathways. Different Kir isoforms display distinct specificities for the activating PIPs but all eukaryotic Kir channels are activated by PI(4,5)P2. On the other hand, the bacterial KirBac1.1 channel is inhibited by PIPs. Recent crystal structures of eukaryotic Kir channels in apo and lipid bound forms reveal one specific binding site per subunit, formed at the interface of N- and C-terminal domains, just beyond the transmembrane segments and clearly involving some of the key residues previously identified as controlling PI(4,5)P2 sensitivity. Computational, biochemical, and biophysical approaches have attempted to address the energetic determinants of PIP binding and selectivity among Kir channel isoforms, as well as the conformational changes that trigger channel gating. Here we review our current understanding of the molecular determinants of PIP regulation of Kir channel activity, including in context with other lipid modulators, and provide further discussion on the key questions that remain to be answered.
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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.