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Article

Identification of subdomains in NADPH oxidase-4 critical for the oxygen-dependent regulation of TASK-1 K+ channels.

American journal of physiology. Cell physiology - 1 Oct 2009

Park Su Jung, Chun Yang-Sook, Park Kyung Sun, Kim Sung Joon, Choi Si-On, Kim Hye-Lim, Park Jong-Wan

Abstract excerpt

Hypoxic inhibition of K+ current is a critical O2-sensing mechanism. Previously, it was demonstrated that the cooperative action of TASK-1 and NADPH oxidase-4 (NOX4) mediated the O2-sensitive K+ current response. Here we addressed the O2-sensing mechanism of NOX4 in terms of TASK-1 regulation. In TASK-1 and NOX4-coexpressing human embryonic kidney 293 cells, hypoxia (5% O2) decreased the amplitude of TASK-1...

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Share to Carbon Monoxide
Share to Cell Hypoxia

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Enzyme Activation

Share to Ferrochelatase

Share to NADPH Oxidases

Share to Oxygen

Share to Potassium Channels, Tandem Pore Domain

Share to Reactive Oxygen Species

Source

Identifiers

PMID: 19657056
DOI: 10.1152/ajpcell.00463.2008

Genes

NOX4
HBD

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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