ArticleThe EMBO journal2005
Kir6.2 mutations causing neonatal diabetes provide new insights into Kir6.2-SUR1 interactions.
Article in The EMBO journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 64 citations in OpenAlex.
- Acute Hypoxia Inhibits KActa physiologica (Oxford, England) · 2026Article
- Automated patch clamp analysis of heterologously expressed Kir6.2/SUR1 and Kir6.1/SUR2B KAmerican journal of physiology. Cell physiology · 2025Article
- Molecular Dynamics Simulation of Kir6.2 Variants Reveals Potential Association with Diabetes Mellitus.Molecules (Basel, Switzerland) · 2024Article
- Structure of an open KNature communications · 2024Article
- 100 YEARS OF INSULIN: A brief history of diabetes genetics: insights for pancreatic beta-cell development and function.The Journal of endocrinology · 2021Review
- New insights into KNature reviews. Endocrinology · 2020Review
- Activation mechanism of ATP-sensitive KeLife · 2019Article
- Anti-diabetic drug binding site in a mammalian KeLife · 2017Article
- Decreases in Gap Junction Coupling Recovers Ca2+ and Insulin Secretion in Neonatal Diabetes Mellitus, Dependent on Beta Cell Heterogeneity and Noise.PLoS computational biology · 2016Article
- Running out of time: the decline of channel activity and nucleotide activation in adenosine triphosphate-sensitive K-channels.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2016Review
- The Nucleotide-Binding Sites of SUR1: A Mechanistic Model.Biophysical journal · 2015Review
- LKB1 couples glucose metabolism to insulin secretion in mice.Diabetologia · 2015Article
- Hypotension due to Kir6.1 gain-of-function in vascular smooth muscle.Journal of the American Heart Association · 2013Article
- A role of the sulfonylurea receptor 1 in endocytic trafficking of ATP-sensitive potassium channels.Traffic (Copenhagen, Denmark) · 2011Article
- Ankyrin-B regulates Kir6.2 membrane expression and function in heart.The Journal of biological chemistry · 2010Article
- K(ATP) channelopathies in the pancreas.Pflugers Archiv : European journal of physiology · 2010Review
- The molecular mechanisms and pharmacotherapy of ATP-sensitive potassium channel gene mutations underlying neonatal diabetes.Pharmacogenomics and personalized medicine · 2010Article
- An in-frame deletion in Kir6.2 (KCNJ11) causing neonatal diabetes reveals a site of interaction between Kir6.2 and SUR1.The Journal of clinical endocrinology and metabolism · 2009Article
- A cytosolic factor that inhibits KATP channels expressed in Xenopus oocytes by impairing Mg-nucleotide activation by SUR1.The Journal of physiology · 2009Article
- Review. SUR1: a unique ATP-binding cassette protein that functions as an ion channel regulator.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2009Review
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
ATP-sensitive K(+) (K(ATP)) channels, comprised of pore-forming Kir6.2 and regulatory SUR1 subunits, play a critical role in regulating insulin secretion. Binding of ATP to Kir6.2 inhibits, whereas interaction of MgATP with SUR1 activates, K(ATP) channels. We tested the functional effects of two Kir6.2 mutations (Y330C, F333I) that cause permanent neonatal diabetes mellitus, by heterologous expression in Xenopus oocytes. Both mutations reduced ATP inhibition and increased whole-cell currents, which in pancreatic beta-cells is expected to reduce insulin secretion and precipitate diabetes. The Y330C mutation reduced ATP inhibition both directly, by impairing ATP binding (and/or transduction), and indirectly, by stabilizing the intrinsic open state of the channel. The F333I mutation altered ATP binding/transduction directly. Both mutations also altered Kir6.2/SUR1 interactions, enhancing the stimulatory effect of MgATP (which is mediated via SUR1). This effect was particularly dramatic for the Kir6.2-F333I mutation, and was abolished by SUR1 mutations that prevent MgATP binding/hydrolysis. Further analysis of F333I heterozygous channels indicated that at least three SUR1 must bind/hydrolyse MgATP to open the mutant K(ATP) channel.
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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.