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Truncation of Kir6.2 produces ATP-sensitive K+ channels in the absence of the sulphonylurea receptor

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  • Stephen J. Tucker

    (University Laboratory of Physiology)

  • Fiona M. Gribble

    (University Laboratory of Physiology)

  • Chao Zhao

    (University Laboratory of Physiology)

  • Stefan Trapp

    (University Laboratory of Physiology)

  • Frances M. Ashcroft

    (University Laboratory of Physiology)

Abstract

ATP-sensitive potassium channels (K-ATP channels) couple cell metabolism to electrical activity and are important in the physiology and pathophysiology of many tissues1. In pancreatic β-cells, K-ATP channels link changes in blood glucose concentration to insulin secretion2. They are also the target for clinically important drugs such as sulphonylureas, which stimulate secretion, and the K+ channel opener diazoxide, which inhibits insulin release3,4. Metabolic regulation of K-ATP channels is mediated by changes in intracellular ATP and Mg-ADP levels, which inhibit and activate the channel, respectively2. The β-cell K-ATP channel is a complex of two proteins5,6: an inward-rectifier K+ channel subunit, Kir6.2, and the sulphonylurea receptor, SUR1. We show here that the primary site at which ATP acts to mediate K-ATP channel inhibition is located on Kir6.2, and that SUR1 is required for sensitivity to sulphonylureas and diazoxide and for activation by Mg-ADP.

Suggested Citation

  • Stephen J. Tucker & Fiona M. Gribble & Chao Zhao & Stefan Trapp & Frances M. Ashcroft, 1997. "Truncation of Kir6.2 produces ATP-sensitive K+ channels in the absence of the sulphonylurea receptor," Nature, Nature, vol. 387(6629), pages 179-183, May.
    • Handle: RePEc:nat:nature:v:387:y:1997:i:6629:d:10.1038_387179a0
    DOI: 10.1038/387179a0
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    Cited by:

    1. Mengmeng Wang & Jing-Xiang Wu & Dian Ding & Lei Chen, 2022. "Structural insights into the mechanism of pancreatic KATP channel regulation by nucleotides," Nature Communications, Nature, vol. 13(1), pages 1-10, December.
    2. Camden M. Driggers & Yi-Ying Kuo & Phillip Zhu & Assmaa ElSheikh & Show-Ling Shyng, 2024. "Structure of an open KATP channel reveals tandem PIP2 binding sites mediating the Kir6.2 and SUR1 regulatory interface," Nature Communications, Nature, vol. 15(1), pages 1-16, December.

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