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- W2090854852 abstract "GIRK channels allow potassium ions to cross the cell membrane, thereby affecting the electrical status of the cell and so its functioning. Structural data now provide insight into the channels' mode of operation. See Article p.190 The activation of G-protein-coupled receptors (GPCRs) leads to the release of the G-protein subunits Gα and Gβγ from the intracellular surface of the GPCR. Gβγ can then bind to, and activate, the G-protein-gated inward rectifier K+ (GIRK) channel, causing the channel pore to open. The opening of GIRK channels drives the membrane voltage towards the resting (Nernst) potential, which slows the rate of membrane depolarization. In this manuscript, Matthew Whorton and Roderick MacKinnon solve the X-ray crystal structure of a mammalian GIRK2 channel in the presence of the βγ G-protein subunits. Although the overall structure of the βγ G-protein subunits is essentially the same in the presence of Gα or GIRK, the structures of GIRK and GIRK–Gβγ are quite different. The structure also reveals how the signalling lipid PIP2 and intracellular Na+ ions help to regulate the activity of GIRKs." @default.
- W2090854852 created "2016-06-24" @default.
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- W2090854852 date "2013-06-05" @default.
- W2090854852 modified "2023-10-18" @default.
- W2090854852 title "Ion channel twists to open" @default.
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- W2090854852 doi "https://doi.org/10.1038/nature12255" @default.
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