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Structure of an open K_ATP channel reveals tandem PIP₂ binding sites mediating the Kir6.2 and SUR1 regulatory interface

K_ATP channels regulate insulin secretion and are activated by PIP₂. Here, the authors show PIP₂ binds between SUR1 and Kir6.2 to open the channel, and a neonatal diabetes mutation stabilizes K_ATP channels in a PIP₂-bound open conformation.

Camden M. Driggers
Yi-Ying Kuo
Show-Ling Shyng
ResearchOpen Access20 Mar 2024
Nature Communications

Volume: 15, P: 1-16

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Structure of an open KATP channel reveals tandem PIP2 binding sites mediating the Kir6.2 and SUR1 regulatory interface

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Structure of an open K_ATP channel reveals tandem PIP₂ binding sites mediating the Kir6.2 and SUR1 regulatory interface