Regions responsible for the assembly of inwardly rectifying potassium channels
Article Abstract:
The mechanics of the inward rectification of potassium channels is investigated. Regions of the protein that trigger homo- and heteromultimerization are analyzed. Biochemical and electrophysiological techniques are used to identify regions needed for homotypic interactions and responsible for incompatibility between IRK1 and two members of the same subfamily and two members from other subfamilies. A region in the proximal C-terminus and the transmembrane segment M2 is found to determine assembly and compatibility.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1996
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Regulation of IRK3 inward rectifier K+ channel by m1 acetylcholine receptor and intracellular magnesium
Article Abstract:
An investigation was conducted on the regulation of IRK3 inward rectifier K+ channel by m1 acetylcholine receptor and intracellular magnesium. This m1 modulation can, however, be replicated by Mg2+. IRK1 mutant channels and quantitative analyses of IRK3 suggest that chronic inhibition of IRK3 channels and m1 receptor stimulation as a result of reposing the level of Mg2+ can cause an enhancement of cytoplasmic Mg2+ concentration. Furthermore, it could lead to channel inhibition.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1997
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Transmembrane structure of an inwardly rectifying potassium channel
Article Abstract:
A study was conducted to determine the transmembrane structure of inwardly rectifying potassium channels with mutagenized M1 and M2 transmembrane domains. Results indicate that M1 and M2 are helices. Using second-site suppressor analyses, it was revealed that M2 pore-lining inner helices are encircled by M1 lipid-facing outer helices. This arrangement allows M1 helices to participate in subunit-subunit interactions.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1999
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