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Sensing voltage across lipid membranes

Author

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  • Kenton J. Swartz

    (Porter Neuroscience Research Center, Molecular Physiology and Biophysics Section, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, Maryland 20892, USA)

Abstract

Voltage sensing by membrane proteins The ability of proteins to detect electrical potentials across biological membranes is critical for many cellular processes, including the generation and propagation of nerve impulses. Ground-breaking structural studies on the 'activated' conformation of voltage-sensing domains have revealed a surprisingly intimate interaction between these protein domains and the surrounding lipid bilayer. Mobile cationic residues within voltage-sensor domains are stabilized within the membrane by interactions with anionic residues and with the phosphate moiety of lipid end groups. Although the structure of the 'resting' conformation of the voltage sensor is anxiously awaited, the available data are consistent with half-bilayer dimension motions of charged residues through a focused electric field. For more background, visit the web focus on http://www.nature.com/nature/focus/voltagesensing/

Suggested Citation

  • Kenton J. Swartz, 2008. "Sensing voltage across lipid membranes," Nature, Nature, vol. 456(7224), pages 891-897, December.
    • Handle: RePEc:nat:nature:v:456:y:2008:i:7224:d:10.1038_nature07620
    DOI: 10.1038/nature07620
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    Cited by:

    1. Purushotham Selvakumar & Ana I. Fernández-Mariño & Nandish Khanra & Changhao He & Alice J. Paquette & Bing Wang & Ruiqi Huang & Vaughn V. Smider & William J. Rice & Kenton J. Swartz & Joel R. Meyerson, 2022. "Structures of the T cell potassium channel Kv1.3 with immunoglobulin modulators," Nature Communications, Nature, vol. 13(1), pages 1-12, December.
    2. Tobias Raisch & Andreas Brockmann & Ulrich Ebbinghaus-Kintscher & Jörg Freigang & Oliver Gutbrod & Jan Kubicek & Barbara Maertens & Oliver Hofnagel & Stefan Raunser, 2021. "Small molecule modulation of the Drosophila Slo channel elucidated by cryo-EM," Nature Communications, Nature, vol. 12(1), pages 1-12, December.

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