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KATP channels as molecular sensors of cellular metabolism

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  • Colin G. Nichols

    (Washington University School of Medicine)

Abstract

In responding to cytoplasmic nucleotide levels, ATP-sensitive potassium (KATP) channel activity provides a unique link between cellular energetics and electrical excitability. Over the past ten years, a steady drumbeat of crystallographic and electrophysiological studies has led to detailed structural and kinetic models that define the molecular basis of channel activity. In parallel, the uncovering of disease-causing mutations of KATP has led to an explanation of the molecular basis of disease and, in turn, to a better understanding of the structural basis of channel function.

Suggested Citation

  • Colin G. Nichols, 2006. "KATP channels as molecular sensors of cellular metabolism," Nature, Nature, vol. 440(7083), pages 470-476, March.
    • Handle: RePEc:nat:nature:v:440:y:2006:i:7083:d:10.1038_nature04711
    DOI: 10.1038/nature04711
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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.
    3. Dian Ding & Tianyi Hou & Miao Wei & Jing-Xiang Wu & Lei Chen, 2023. "The inhibition mechanism of the SUR2A-containing KATP channel by a regulatory helix," Nature Communications, Nature, vol. 14(1), pages 1-12, December.
    4. Tobias Linder & Bert L de Groot & Anna Stary-Weinzinger, 2013. "Probing the Energy Landscape of Activation Gating of the Bacterial Potassium Channel KcsA," PLOS Computational Biology, Public Library of Science, vol. 9(5), pages 1-9, May.
    5. Dian Ding & Jing-Xiang Wu & Xinli Duan & Songling Ma & Lipeng Lai & Lei Chen, 2022. "Structural identification of vasodilator binding sites on the SUR2 subunit," Nature Communications, Nature, vol. 13(1), pages 1-9, December.

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