ArticleThe Journal of general physiology2012
Engineered interaction between SUR1 and Kir6.2 that enhances ATP sensitivity in KATP channels.
Article in The Journal of general physiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 40 citations in OpenAlex.
- Inhibition Mechanism of Pancreatic KResearch (Washington, D.C.) · 2026Article
- Dynamic duo: Kir6 and SUR in KChannels (Austin, Tex.) · 2024Review
- HCV affects KEndocrine · 2024Article
- Structure of an open KNature communications · 2024Article
- Electro-metabolic signaling.The Journal of general physiology · 2024Article
- KCurrent opinion in structural biology · 2023Review
- Mechanistic insights on KATP channel regulation from cryo-EM structures.The Journal of general physiology · 2023Review
- Ligand-mediated Structural Dynamics of a Mammalian Pancreatic KJournal of molecular biology · 2022Article
- Structural insights into the mechanism of pancreatic KNature communications · 2022Article
- Molecular structure of an open human KProceedings of the National Academy of Sciences of the United States of America · 2021Article
- Development of IFrontiers in pharmacology · 2021Article
- Production and purification of ATP-sensitive potassium channel particles for cryo-electron microscopy.Methods in enzymology · 2021Article
- New insights into KNature reviews. Endocrinology · 2020Review
- Nucleotide inhibition of the pancreatic ATP-sensitive K+ channel explored with patch-clamp fluorometry.eLife · 2020Article
- Article
- Cryo-electron microscopy structures and progress toward a dynamic understanding of KThe Journal of general physiology · 2018Review
- Article
- Anti-diabetic drug binding site in a mammalian KeLife · 2017Article
- Cryo-EM structure of the ATP-sensitive potassium channel illuminates mechanisms of assembly and gating.eLife · 2017Article
- Structural basis of control of inward rectifier Kir2 channel gating by bulk anionic phospholipids.The Journal of general physiology · 2016Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The ATP-sensitive potassium (K(ATP)) channel consisting of the inward rectifier Kir6.2 and SUR1 (sulfonylurea receptor 1) couples cell metabolism to membrane excitability and regulates insulin secretion. Inhibition by intracellular ATP is a hallmark feature of the channel. ATP sensitivity is conferred by Kir6.2 but enhanced by SUR1. The mechanism by which SUR1 increases channel ATP sensitivity is not understood. In this study, we report molecular interactions between SUR1 and Kir6.2 that markedly alter channel ATP sensitivity. Channels bearing an E203K mutation in SUR1 and a Q52E in Kir6.2 exhibit ATP sensitivity ∼100-fold higher than wild-type channels. Cross-linking of E203C in SUR1 and Q52C in Kir6.2 locks the channel in a closed state and is reversible by reducing agents, demonstrating close proximity of the two residues. Our results reveal that ATP sensitivity in K(ATP) channels is a dynamic parameter dictated by interactions between SUR1 and Kir6.2.
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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.