Cited by 417Ion channel regulation and functionLipid Membrane Structure and BehaviorIon Transport and Channel Regulation

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Phospholipids and the origin of cationic gating charges in voltage sensors

Schmidt, Daniel, Jiang, Qiu-Xing, MacKinnon, Roderick·2006·Nature

DOI 10.1038/nature05416

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Abstract

Cells communicate with their external environment through physical and chemical processes that take place in the cell-surrounding membrane. The membrane serves as a barrier as well as a special environment in which membrane proteins are able to carry out important processes. Certain membrane proteins have the ability to detect the membrane voltage and regulate ion conduction or enzyme activity. Such voltage-dependent processes rely on the action of protein domains known as voltage sensors, which are embedded inside the cell membrane and contain an excess of positively charged amino acids, which react to an electric field. How does the membrane create an environment suitable for voltage sensors? Here we show under a variety of conditions that the function of a voltage-dependent K+ channel is dependent on the negatively charged phosphodiester of phospholipid molecules. A non-voltage-dependent K+ channel does not exhibit the same dependence. The data lead us to propose that the phospholipid membrane, by providing stabilizing interactions between positively charged voltage-sensor arginine residues and negatively charged lipid phosphodiester groups, provides an appropriate environment for the energetic stability and operation of the voltage-sensing machinery. We suggest that the usage of arginine residues in voltage sensors is an adaptation to the phospholipid composition of cell membranes.

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Authors: Schmidt, D., Jiang, Q.-X., & MacKinnon, R.
Affiliations: Howard Hughes Medical Institute (US)
Corresponding author: MacKinnon, Roderick
ORCID: Schmidt, Daniel
Jiang, Qiu-Xing
MacKinnon, Roderick
Venue: Nature
Publisher: Springer Science and Business Media LLC
Published: 2006-11-29
Volume: 444
Issue: 7120
Pages: 775-779
ISSN: 0028-0836 (ISSN-L)
1476-4687
DOI: 10.1038/nature05416
OpenAlex: W2022309859
Cited by: 417
References: 21
Citations by year: 2026: 8 · 2025: 10 · 2024: 11 · 2023: 7 · 2022: 8 · 2021: 11 · 2020: 14 · 2019: 18 · 2018: 16 · 2017: 13 · 2016: 14 · 2015: 19 · 2014: 36 · 2013: 29 · 2012: 32
FWCI: 13.31
Type: journal article
Language: en
Open access: closed
Licence: www.springer.com/tdm (tdm)
Locations: Nature (publishedVersion)
PubMed (publishedVersion)
RePEc: Research Papers in Economics (submittedVersion)
Funders: Howard Hughes Medical Institute
National Institutes of Health
National Institute of General Medical Sciences (R01GM043949)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ion channel regulation and function
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Lipid Membrane Structure and Behavior
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ion Transport and Channel Regulation
Keywords: voltage sensor, phospholipids, potassium channels, arginine residues, membrane lipid composition, membrane potential, voltage-gated ion channels, membrane protein stability
MeSH terms: Cations, Lipid Bilayers, Liposomes, Phospholipids, Ion Channel Gating, Potassium Channels, Voltage-Gated

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Phospholipids and the origin of cationic gating charges in voltage sensors

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