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Article

Impact of disease-causing SUR1 mutations on the KATP channel subunit interface probed with a rhodamine protection assay.

The Journal of biological chemistry - 29 Jan 2010

Hosy Eric, Dupuis Julien P, Vivaudou Michel

Abstract excerpt

The function of the ATP-sensitive potassium (K(ATP)) channel relies on the proper coupling between its two subunits: the pore-forming Kir6.2 and the regulator SUR. The conformation of the interface between these two subunits can be monitored using a rhodamine 123 (Rho) protection assay because Rho blocks Kir6.2 with an efficiency that depends on the relative position of transmembrane domain (TMD) 0 of the...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 19933268
DOI: 10.1074/jbc.M109.043307
PMCID: PMC2823424

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

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Impact of disease-causing SUR1 mutations on the KATP channel subunit interface probed with a rhodamine protection assay.PMID 19933268Read ↗

Remodelling of the SUR-Kir6.2 interface of the KATP channel upon ATP binding revealed by the conformational blocker rhodamine 123.Semantic proximity Read ↗

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A conserved tryptophan at the membrane-water interface acts as a gatekeeper for Kir6.2/SUR1 channels and causes neonatal diabetes when mutated.Semantic proximity Read ↗

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