ArticleThe Journal of general physiology2000
Structural determinants of PIP(2) regulation of inward rectifier K(ATP) channels.
Article in The Journal of general physiology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 104 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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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
104 citing papers in PubMed, 207 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
- Dynamic duo: Kir6 and SUR in KChannels (Austin, Tex.) · 2024Review
- Exploring the Pathophysiology of ATP-Dependent Potassium Channels in Insulin Resistance.International journal of molecular sciences · 2024Review
- Cloning, functional expression, and pharmacological characterization of inwardly rectifying potassium channels (Kir) from Apis mellifera.Scientific reports · 2024Article
- Mechanistic insights on KATP channel regulation from cryo-EM structures.The Journal of general physiology · 2023Review
- CL-705G: a novel chemical Kir6.2-specific KFrontiers in pharmacology · 2023Article
- Cholesterol and PIPAdvances in experimental medicine and biology · 2023Article
- Ligand-mediated Structural Dynamics of a Mammalian Pancreatic KJournal of molecular biology · 2022Article
- The dynamic interplay of PIPThe Journal of physiology · 2022Article
- From Bench to Biomolecular Simulation: Phospholipid Modulation of Potassium Channels.Journal of molecular biology · 2021Review
- Distinct lipid bilayer compositions have general and protein-specific effects on K+ channel function.The Journal of general physiology · 2021Article
- Simulating PIPFrontiers in molecular biosciences · 2021Article
- Production and purification of ATP-sensitive potassium channel particles for cryo-electron microscopy.Methods in enzymology · 2021Article
- Tetraspanin-7 regulation of L-type voltage-dependent calcium channels controls pancreatic β-cell insulin secretion.The Journal of physiology · 2020Article
- New insights into KNature reviews. Endocrinology · 2020Review
- Palmitoylation of the KProceedings of the National Academy of Sciences of the United States of America · 2020Article
- Lipid Interactions of a Ciliary Membrane TRP Channel: Simulation and Structural Studies of Polycystin-2.Structure (London, England : 1993) · 2020Article
- Novel dominant KAmerican journal of medical genetics. Part A · 2019Article
- Anionic Phospholipids Bind to and Modulate the Activity of Human TRESK Background KMolecular neurobiology · 2019Article
- Depletion of plasma membrane-associated phosphoinositides mimics inhibition of TRPM7 channels by cytosolic MgThe Journal of biological chemistry · 2018Article
44 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Phosphatidylinositol 4,5-bisphosphate (PIP(2)) activates K(ATP) and other inward rectifier (Kir) channels. To determine residues important for PIP(2) regulation, we have systematically mutated each positive charge in the COOH terminus of Kir6.2 to alanine. The effects of these mutations on channel function were examined using (86)Rb efflux assays on intact cells and inside-out patch-clamp methods. Both methods identify essentially the same basic residues in two narrow regions (176-222 and 301-314) in the COOH terminus that are important for the maintenance of channel function and interaction with PIP(2). Only one residue (R201A) simultaneously affected ATP and PIP(2) sensitivity, which is consistent with the notion that these ligands, while functionally competitive, are unlikely to bind to identical sites. Strikingly, none of 13 basic residues in the terminal portion (residues 315-390) of the COOH terminus affected channel function when neutralized. The data help to define the structural requirements for PIP(2) sensitivity of K(ATP) channels. Moreover, the regions and residues defined in this study parallel those uncovered in recent studies of PIP(2) sensitivity in other inward rectifier channels, indicating a common structural basis for PIP(2) regulation.
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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.