ArticleThe Journal of general physiology2001
Mutations within the P-loop of Kir6.2 modulate the intraburst kinetics of the ATP-sensitive potassium channel.
Article in The Journal of general physiology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
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Who cites it
44 citing papers in PubMed.
- Inward and outward currents of native and cloned K(ATP) channels (Kir6.2/SUR1) share single-channel kinetic properties.Biochemistry and biophysics reports · 2022Article
- Correlation between structure and function in phosphatidylinositol lipid-dependent Kir2.2 gating.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Molecular structure of an open human KProceedings of the National Academy of Sciences of the United States of America · 2021Article
- Structural Determinants of Insulin Release: Disordered N-Terminal Tail of Kir6.2 Affects Potassium Channel Dynamics through Interactions with Sulfonylurea Binding Region in a SUR1 Partner.The journal of physical chemistry. B · 2020Article
- Conformational changes upon gating of KirBac1.1 into an open-activated state revealed by solid-state NMR and functional assays.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Atomistic basis of opening and conduction in mammalian inward rectifier potassium (Kir2.2) channels.The Journal of general physiology · 2020Article
- Control of Kir channel gating by cytoplasmic domain interface interactions.The Journal of general physiology · 2017Article
- Emergence of ion channel modal gating from independent subunit kinetics.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Hyperinsulinemic Hypoglycemia - The Molecular Mechanisms.Frontiers in endocrinology · 2016Review
- Aromatic-aromatic interactions between residues in KCa3.1 pore helix and S5 transmembrane segment control the channel gating process.The Journal of general physiology · 2014Article
- A Kir6.2 pore mutation causes inactivation of ATP-sensitive potassium channels by disrupting PIP2-dependent gating.PloS one · 2013Article
- Neuroprotective role of ATP-sensitive potassium channels in cerebral ischemia.Acta pharmacologica Sinica · 2013Review
- Differential regulation of the InsP₃ receptor type-1 and -2 single channel properties by InsP₃, Ca²⁺ and ATP.The Journal of physiology · 2012Article
- Protein kinase C mediated pH(i)-regulation of ROMK1 channels via a phosphatidylinositol-4,5-bisphosphate-dependent mechanism.Journal of molecular modeling · 2012Article
- Current understanding of K ATP channels in neonatal diseases: focus on insulin secretion disorders.Acta pharmacologica Sinica · 2011Review
- A multipoint hydrogen-bond network underlying KcsA C-type inactivation.Biophysical journal · 2011Article
- On the structural basis of modal gating behavior in K(+) channels.Nature structural & molecular biology · 2011Article
- Activation of the K(ATP) channel by Mg-nucleotide interaction with SUR1.The Journal of general physiology · 2010Article
- Structural basis for the coupling between activation and inactivation gates in K(+) channels.Nature · 2010Article
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4 authors.
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Abstract
The ATP-sensitive potassium (K(ATP)) channel exhibits spontaneous bursts of rapid openings, which are separated by long closed intervals. Previous studies have shown that mutations at the internal mouth of the pore-forming (Kir6.2) subunit of this channel affect the burst duration and the long interburst closings, but do not alter the fast intraburst kinetics. In this study, we have investigated the nature of the intraburst kinetics by using recombinant Kir6.2/SUR1 K(ATP) channels heterologously expressed in Xenopus oocytes. Single-channel currents were studied in inside-out membrane patches. Mutations within the pore loop of Kir6.2 (V127T, G135F, and M137C) dramatically affected the mean open time (tau(o)) and the short closed time (tauC1) within a burst, and the number of openings per burst, but did not alter the burst duration, the interburst closed time, or the channel open probability. Thus, the V127T and M137C mutations produced longer tau(o), shorter tauC1, and fewer openings per burst, whereas the G135F mutation had the opposite effect. All three mutations also reduced the single-channel conductance: from 70 pS for the wild-type channel to 62 pS (G135F), 50 pS (M137C), and 38 pS (V127T). These results are consistent with the idea that the K(ATP) channel possesses a gate that governs the intraburst kinetics, which lies close to the selectivity filter. This gate appears to be able to operate independently of that which regulates the long interburst closings.
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