Article

Extracellular cysteine disulfide bond break at Cys122 disrupts PIP <sub>2</sub> -dependent Kir2.1 channel function and leads to arrhythmias in Andersen-Tawil Syndrome

2023-06-09

Abstract excerpt

<h4>Background</h4> Andersen-Tawil Syndrome Type 1 (ATS1) is a rare heritable disease caused by mutations in the strong inwardly rectifying K + channel Kir2.1. The extracellular Cys122-to-Cys154 disulfide bond in the Kir2.1 channel structure is crucial for proper folding, but has not been associated with correct channel function at the membrane. We tested whether a human mutation at the Cys122-to-Cys154 disulfid...

Topics

Open a Topic to create a Post that cites this publication.

Identifiers and source

Literature Corpus work: b83c9f10-fd96-53c0-89b3-2324d171d8aa
DOI: 10.1101/2023.06.07.544151

Open publication

Related research

Semantic proximity does not establish scientific evidence.

Click a neighbor to travelStep 1 · 12 closest

Extracellular cysteine disulfide bond break at Cys122 disrupts PIP <sub>2</sub> -dependent Kir2.1 channel function and leads to arrhythmias in Andersen-Tawil SyndromeDOI 10.1101/2023.06.07.544151Read

Extracellular Kir2.1C122Y Mutant Upsets Kir2.1-PIP2 Bonds and Is Arrhythmogenic in Andersen-Tawil Syndrome.Semantic proximity Read

Two critical cysteine residues implicated in disulfide bond formation and proper folding of Kir2.1.Semantic proximity Read

Biochemical, biophysical, and structural investigations of two mutants (C154Y and R312H) of the human Kir2.1 channel involved in the Andersen-Tawil syndromeSemantic proximity Read

Biochemical, biophysical, and structural investigations of two mutants (C154Y and R312H) of the human Kir2.1 channel involved in the Andersen-Tawil syndrome.Semantic proximity Read

Single Ion Pair Is Essential for Stabilizing SHP2's Open Conformation.Semantic proximity Read

Conserved cysteine residues in the extracellular loop of the human P2X(1) receptor form disulfide bonds and are involved in receptor trafficking to the cell surface.Semantic proximity Read

Distant cytosolic residues mediate a two-way molecular switch that controls the modulation of inwardly rectifying potassium (Kir) channels by cholesterol and phosphatidylinositol 4,5-bisphosphate (PI(4,5)P(2)).Semantic proximity Read

Contribution of cytosolic cysteine residues to the gating properties of the Kir2.1 inward rectifier.Semantic proximity Read

Identification of a disulfide bridge essential for structure and function of the voltage-gated Ca(2+) channel α(2)δ-1 auxiliary subunit.Semantic proximity Read

Localization of a disease-associated mutation site in the three-dimensional structure of the cardiac muscle ryanodine receptor.Semantic proximity Read

Claudin-2 pore function requires an intramolecular disulfide bond between two conserved extracellular cysteines.Semantic proximity Read

Identification of the cysteine residue responsible for disulfide linkage of Na+ channel α and β2 subunits.Semantic proximity Read