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Article

N-terminal transmembrane domain of SUR1 controls gating of Kir6.2 by modulating channel sensitivity to PIP2.

The Journal of general physiology - 1 Mar 2011

Pratt Emily B, Tewson Paul, Bruederle Cathrin E, Skach William R, Shyng Show-Ling

Abstract excerpt

Functional integrity of pancreatic adenosine triphosphate (ATP)-sensitive potassium (K(ATP)) channels depends on the interactions between the pore-forming potassium channel subunit Kir6.2 and the regulatory subunit sulfonylurea receptor 1 (SUR1). Previous studies have shown that the N-terminal transmembrane domain of SUR1 (TMD0) interacts with Kir6.2 and is sufficient to confer high intrinsic open probability...

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Share to Glutamic Acid
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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to KATP Channels

Share to Membrane Potentials

Share to Phosphatidylinositol 4,5-Diphosphate

Share to Potassium Channels, Inwardly Rectifying

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Source

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Identifiers

PMID: 21321069
DOI: 10.1085/jgp.201010557
PMCID: PMC3047609

Genes

PIP

Variants

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Related research

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Research trail→

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N-terminal transmembrane domain of SUR1 controls gating of Kir6.2 by modulating channel sensitivity to PIP2.PMID 21321069Read ↗

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Identification and Rescue of Congenital Hyperinsulinism-Associated <i>ABCC8</i> Mutations that Impair K <sub>ATP</sub> Channel TraffickingSemantic proximity Read ↗

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

Kir6.2 mutations associated with neonatal diabetes reduce expression of ATP-sensitive K+ channels: implications in disease mechanism and sulfonylurea therapy.Semantic proximity Read ↗

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

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