ArticleThe Journal of physiology2006
The N-terminal transmembrane domain (TMD0) and a cytosolic linker (L0) of sulphonylurea receptor define the unique intrinsic gating of KATP channels.
Article in The Journal of physiology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 37 citations in OpenAlex.
- A Cantú syndrome mutation produces dual effects on KATP channels by disrupting ankyrin B regulation.The Journal of general physiology · 2023Article
- Nucleotide inhibition of the pancreatic ATP-sensitive K+ channel explored with patch-clamp fluorometry.eLife · 2020Article
- Glibenclamide and HMR1098 normalize Cantú syndrome-associated gain-of-function currents.Journal of cellular and molecular medicine · 2019Article
- Expression, purification, and electrophysiological characterization of a recombinant, fluorescent Kir6.2 in mammalian cells.Protein expression and purification · 2018Article
- Cryo-electron microscopy structures and progress toward a dynamic understanding of KThe Journal of general physiology · 2018Review
- Cantu syndrome-associated SUR2 (ABCC9) mutations in distinct structural domains result in KThe Journal of biological chemistry · 2018Article
- New insights into the roles of the N-terminal region of the ABCC6 transporter.Journal of bioenergetics and biomembranes · 2016Article
- Phosphorylation-dependent changes in nucleotide binding, conformation, and dynamics of the first nucleotide binding domain (NBD1) of the sulfonylurea receptor 2B (SUR2B).The Journal of biological chemistry · 2015Article
- Kir6.2 activation by sulfonylurea receptors: a different mechanism of action for SUR1 and SUR2A subunits via the same residues.Physiological reports · 2015Article
- Measuring and evaluating the role of ATP-sensitive K+ channels in cardiac muscle.Journal of molecular and cellular cardiology · 2012Review
- Role of the amino-terminal transmembrane domain of sulfonylurea receptor SUR2B for coupling to K(IR)6.2, ligand binding, and oligomerization.Naunyn-Schmiedeberg's archives of pharmacology · 2012Article
- Current understanding of K ATP channels in neonatal diseases: focus on insulin secretion disorders.Acta pharmacologica Sinica · 2011Review
- The molecular mechanisms and pharmacotherapy of ATP-sensitive potassium channel gene mutations underlying neonatal diabetes.Pharmacogenomics and personalized medicine · 2010Article
- Coassembly of different sulfonylurea receptor subtypes extends the phenotypic diversity of ATP-sensitive potassium (KATP) channels.Molecular pharmacology · 2008Article
- How ATP inhibits the open K(ATP) channel.The Journal of general physiology · 2008Article
- Three C-terminal residues from the sulphonylurea receptor contribute to the functional coupling between the K(ATP) channel subunits SUR2A and Kir6.2.The Journal of physiology · 2008Article
- Role for SUR2A ED domain in allosteric coupling within the K(ATP) channel complex.The Journal of general physiology · 2008Article
- Sulfonylurea receptors type 1 and 2A randomly assemble to form heteromeric KATP channels of mixed subunit composition.The Journal of general physiology · 2008Article
- Mutations in the ABCC8 gene encoding the SUR1 subunit of the KATP channel cause transient neonatal diabetes, permanent neonatal diabetes or permanent diabetes diagnosed outside the neonatal period.Diabetes, obesity & metabolism · 2007Article
- Remodelling of the SUR-Kir6.2 interface of the KATP channel upon ATP binding revealed by the conformational blocker rhodamine 123.The Journal of physiology · 2007Article
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
Abstract
ATP-sensitive potassium (K(ATP)) channels comprise four pore-forming Kir6 and four regulatory sulphonylurea receptor (SUR) subunits. SUR, an ATP-binding cassette protein, associates with Kir6 through its N-terminal transmembrane domain (TMD0). TMD0 connects to the core domain of SUR through a cytosolic linker (L0). The intrinsic gating of Kir6.2 is greatly altered by SUR. It has been hypothesized that these changes are conferred by TMD0. Exploiting the fact that the pancreatic (SUR1/Kir6.2) and the cardiac (SUR2A/Kir6.2) K(ATP) channels show different gating behaviours, we have tested this hypothesis by comparing the intrinsic gating of Kir6.2 with the last 26 residues deleted (Kir6.2Delta26) co-expressed with SUR1, S1-TMD0, SUR2A and S2-TMD0 at -40 and -100 mV (S is an abbreviation for SUR; TMD0/Kir6.2Delta26, but not TMD0/Kir6.2, can exit the endoplastic reticulum and reach the cell membrane). Single-channel kinetic analyses revealed that the mean burst and interburst durations are shorter for TMD0/Kir6.2Delta26 than for the corresponding SUR channels. No differences were found between the two TMD0 channels. We further demonstrated that in isolation even TMD0-L0 (SUR truncated after L0) cannot confer the wild-type intrinsic gating to Kir6.2Delta26 and that swapping L0 (SUR truncated after L0)between SUR1 and SUR2A only partially exchanges their different intrinsic gating. Therefore, in addition to TMD0, L0 and the core domain also participate in determining the intrinsic gating of Kir6.2. However, TMD0 and L0 are responsible for the different gating patterns of full-length SUR1 and SUR2A channels. A kinetic model with one open and four closed states is presented to explain our results in a mechanistic context.
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