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Article

MgATP activates the beta cell KATP channel by interaction with its SUR1 subunit.

Proceedings of the National Academy of Sciences of the United States of America - 9 Jun 1998

Gribble F M, Tucker S J, Haug T, Ashcroft F M

Abstract excerpt

ATP-sensitive potassium (KATP) channels in the pancreatic beta cell membrane mediate insulin release in response to elevation of plasma glucose levels. They are open at rest but close in response to glucose metabolism, producing a depolarization that stimulates Ca2+ influx and exocytosis. Metabolic regulation of KATP channel activity currently is believed to be mediated by changes in the intracellular...

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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

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Identifiers

PMID: 9618560
DOI: 10.1073/pnas.95.12.7185
PMCID: PMC22779

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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MgATP activates the beta cell KATP channel by interaction with its SUR1 subunit.PMID 9618560Read ↗

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The Kir6.2-F333I mutation differentially modulates KATP channels composed of SUR1 or SUR2 subunits.Semantic proximity Read ↗

The Pharmacology of ATP-Sensitive K+ Channels (KATP).Semantic proximity Read ↗

Functional effects of naturally occurring KCNJ11 mutations causing neonatal diabetes on cloned cardiac KATP channels.Semantic proximity Read ↗

A universally conserved residue in the SUR1 subunit of the KATP channel is essential for translating nucleotide binding at SUR1 into channel opening.Semantic proximity Read ↗

Kir6.2 mutations causing neonatal diabetes provide new insights into Kir6.2-SUR1 interactions.Semantic proximity Read ↗

Differential response of K(ATP) channels containing SUR2A or SUR2B subunits to nucleotides and pinacidil.Semantic proximity Read ↗

A mutation in the ATP-binding site of the Kir6.2 subunit of the KATP channel alters coupling with the SUR2A subunit.Semantic proximity Read ↗

A mutation (R826W) in nucleotide-binding domain 1 of ABCC8 reduces ATPase activity and causes transient neonatal diabetes.Semantic proximity Read ↗

Focus on Kir6.2: a key component of the ATP-sensitive potassium channel.Semantic proximity Read ↗

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