Kv7.1 ion channels require a lipid to couple voltage sensing to pore opening. - Wikidata - wikimedia - TriplyDB

Kv7.1 ion channels require a lipid to couple voltage sensing to pore opening.

Kv7.1 ion channels require a lipid to couple voltage sensing to pore opening.

http://www.wikidata.org/entity/Q37088789

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The KCNQ1 channel - remarkable flexibility in gating allows for functional versatility KCNQ1 channel modulation by KCNE proteins via the voltage-sensing domain Lipid agonism: The PIP2 paradigm of ligand-gated ion channels Regulation of KCNQ/Kv7 family voltage-gated K+ channels by lipids.Novel Kv7.1-phosphatidylinositol 4,5-bisphosphate interaction sites uncovered by charge neutralization scanning PIP₂-dependent coupling is prominent in Kv7.1 due to weakened interactions between S4-S5 and S6.Probing binding sites and mechanisms of action of an I(Ks) activator by computations and experiments.A long QT mutation substitutes cholesterol for phosphatidylinositol-4,5-bisphosphate in KCNQ1 channel regulation.Major diversification of voltage-gated K+ channels occurred in ancestral parahoxozoans.Phosphoinositides regulate ion channels.Domain-domain interactions determine the gating, permeation, pharmacology, and subunit modulation of the IKs ion channel Phosphatidylinositol 4,5-bisphosphate depletion fails to affect neurosteroid modulation of GABAA receptor function.Functional Characterization of Cnidarian HCN Channels Points to an Early Evolution of Ih.Marginally hydrophobic transmembrane α-helices shaping membrane protein folding.Migration of PIP2 lipids on voltage-gated potassium channel surface influences channel deactivation Bimodal regulation of an Elk subfamily K+ channel by phosphatidylinositol 4,5-bisphosphate.bSUM: A bead-supported unilamellar membrane system facilitating unidirectional insertion of membrane proteins into giant vesicles.KCNE3 acts by promoting voltage sensor activation in KCNQ1.Intracellular ATP binding is required to activate the slowly activating K+ channel I(Ks)Short-chain phosphoinositide partitioning into plasma membrane models Building KCNQ1/KCNE1 channel models and probing their interactions by molecular-dynamics simulations.Dynamic PIP2 interactions with voltage sensor elements contribute to KCNQ2 channel gating Lipid bilayer modules as determinants of K+ channel gating.Intracellular bicarbonate regulates action potential generation via KCNQ channel modulation Gating mechanisms underlying deactivation slowing by two KCNQ1 atrial fibrillation mutations.PIP2 regulation of KCNQ channels: biophysical and molecular mechanisms for lipid modulation of voltage-dependent gating.Voltage-Dependent Gating: Novel Insights from KCNQ1 Channels.Molecular Basis of Cardiac Delayed Rectifier Potassium Channel Function and Pharmacology.Cardiac Delayed Rectifier Potassium Channels in Health and Disease.Modulation of Kv7 channels and excitability in the brain.Molecular Pathophysiology of Congenital Long QT Syndrome.Competition of calcified calmodulin N lobe and PIP2 to an LQT mutation site in Kv7.1 channel.SUMOylation determines the voltage required to activate cardiac IKs channels.Early-onset epileptic encephalopathy caused by a reduced sensitivity of Kv7.2 potassium channels to phosphatidylinositol 4,5-bisphosphate.Ca(2+)-Calmodulin and PIP2 interactions at the proximal C-terminus of Kv7 channels.Phosphatidylinositol-4,5-bisphosphate is required for KCNQ1/KCNE1 channel function but not anterograde trafficking.A complex partnership: KCNQ1 and KCNE1.Potassium channels in the heart: structure, function and regulation.Endoplasmic Reticulum-Plasma Membrane Contacts Regulate Cellular Excitability.PIP2 mediates functional coupling and pharmacology of neuronal KCNQ channels.

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Kv7.1 ion channels require a lipid to couple voltage sensing to pore opening.

http://www.wikidata.org/entity/Q37088789

description

article científic

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article scientifique

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articolo scientifico

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artigo científico

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bilimsel makale

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scientific article published on 16 July 2013

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vedecký článok

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vetenskaplig artikel

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videnskabelig artikel

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vědecký článek

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name

Kv7.1 ion channels require a lipid to couple voltage sensing to pore opening.

@en

Kv7.1 ion channels require a lipid to couple voltage sensing to pore opening.

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type

label

Kv7.1 ion channels require a lipid to couple voltage sensing to pore opening.

@en

Kv7.1 ion channels require a lipid to couple voltage sensing to pore opening.

@nl

prefLabel

Kv7.1 ion channels require a lipid to couple voltage sensing to pore opening.

@en

Kv7.1 ion channels require a lipid to couple voltage sensing to pore opening.

@nl

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PNAS.1305167110

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Proceedings of the National Academy of Sciences of the United States of America

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Kv7.1 ion channels require a lipid to couple voltage sensing to pore opening

@en

P2093

H Peter Larsson

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Hongwu Liang

http://www.w3.org/2001/XMLSchema#string

Jianmin Cui

http://www.w3.org/2001/XMLSchema#string

Jingyi Shi

http://www.w3.org/2001/XMLSchema#string

Kelli Delaloye

http://www.w3.org/2001/XMLSchema#string

Mark A Zaydman

http://www.w3.org/2001/XMLSchema#string

Yang Li

http://www.w3.org/2001/XMLSchema#string

P2860

A voltage-gated proton-selective channel lacking the pore domain

A voltage sensor-domain protein is a voltage-gated proton channel

Positional cloning of a novel potassium channel gene: KVLQT1 mutations cause cardiac arrhythmias

Coassembly of K(V)LQT1 and minK (IsK) proteins to form cardiac I(Ks) potassium channel

Structural basis of PIP2 activation of the classical inward rectifier K+ channel Kir2.2

Atomic structure of a voltage-dependent K+ channel in a lipid membrane-like environment

The crystal structure of a voltage-gated sodium channel

Crystal Structure of the Mammalian GIRK2 K+ Channel and Gating Regulation by G Proteins, PIP2, and Sodium

Spectrum of mutations in long-QT syndrome genes. KVLQT1, HERG, SCN5A, KCNE1, and KCNE2

Crystal structure of a mammalian voltage-dependent Shaker family K+ channel

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13180-13185

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scholarly article

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10.1073/PNAS.1305167110

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32

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110

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Jonathan R. Silva

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2013-07-16T00:00:00Z

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249967314

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23861489

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3740903

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