ArticleBiophysical journal2004
Concerted gating mechanism underlying KATP channel inhibition by ATP.
Article in Biophysical journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed.
- Integrative Study of the Structural and Dynamical Properties of a KirBac3.1 Mutant: Functional Implication of a Highly Conserved Tryptophan in the Transmembrane Domain.International journal of molecular sciences · 2021Article
- Production and purification of ATP-sensitive potassium channel particles for cryo-electron microscopy.Methods in enzymology · 2021Article
- Nucleotide inhibition of the pancreatic ATP-sensitive K+ channel explored with patch-clamp fluorometry.eLife · 2020Article
- Role of the C-terminus of SUR in the differential regulation of β-cell and cardiac KThe Journal of physiology · 2018Article
- Oxidative Modification and Its Implications for the Neurodegeneration of Parkinson's Disease.Molecular neurobiology · 2017Review
- The Nucleotide-Binding Sites of SUR1: A Mechanistic Model.Biophysical journal · 2015Review
- A Conserved Residue Cluster That Governs Kinetics of ATP-dependent Gating of Kir6.2 Potassium Channels.The Journal of biological chemistry · 2015Article
- Pharmacological rescue of trafficking-impaired ATP-sensitive potassium channels.Frontiers in physiology · 2013Review
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- Neuroprotective role of ATP-sensitive potassium channels in cerebral ischemia.Acta pharmacologica Sinica · 2013Review
- A conserved tryptophan at the membrane-water interface acts as a gatekeeper for Kir6.2/SUR1 channels and causes neonatal diabetes when mutated.The Journal of physiology · 2011Article
- Current understanding of K ATP channels in neonatal diseases: focus on insulin secretion disorders.Acta pharmacologica Sinica · 2011Review
- How ATP inhibits the open K(ATP) channel.The Journal of general physiology · 2008Article
- Base of pore loop is important for rectification, activation, permeation, and block of Kir3.1/Kir3.4.Biophysical journal · 2006Article
- Kir6.2 channel gating by intracellular protons: subunit stoichiometry for ligand binding and channel gating.The Journal of membrane biology · 2006Article
- Ligand-dependent linkage of the ATP site to inhibition gate closure in the KATP channel.The Journal of general physiology · 2005Article
- ATP-sensitive K+ channel channel/enzyme multimer: metabolic gating in the heart.Journal of molecular and cellular cardiology · 2005Review
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
KATP channels assemble from four regulatory SUR1 and four pore-forming Kir6.2 subunits. At the single-channel current level, ATP-dependent gating transitions between the active burst and the inactive interburst conformations underlie inhibition of the KATP channel by intracellular ATP. Previously, we identified a slow gating mutation, T171A in the Kir6.2 subunit, which dramatically reduces rates of burst to interburst transitions in Kir6.2DeltaC26 channels without SUR1 in the absence of ATP. Here, we constructed all possible mutations at position 171 in Kir6.2DeltaC26 channels without SUR1. Only four substitutions, 171A, 171F, 171H, and 171S, gave rise to functional channels, each increasing Ki,ATP for ATP inhibition by >55-fold and slowing gating to the interburst by >35-fold. Moreover, we investigated the role of individual Kir6.2 subunits in the gating by comparing burst to interburst transition rates of channels constructed from different combinations of slow 171A and fast T171 "wild-type" subunits. The relationship between gating transition rate and number of slow subunits is exponential, which excludes independent gating models where any one subunit is sufficient for inhibition gating. Rather, our results support mechanisms where four ATP sites independently can control a single gate formed by the concerted action of all four Kir6.2 subunit inner helices of the KATP channel.
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