The DOI matches its Crossref record; 21 of the 21 references it cites were found in a registry or an index.
Phospholipids and the origin of cationic gating charges in voltage sensors
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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“In addition, a shift in the ratio of specific GPL subclasses can affect membrane properties such as its fluidity and curvature, 25 which can further modulate neuronal excitability.45,47,71”
From Large neutral amino acid levels tune perinatal neuronal excitability and survival (2023) · cites this paper as [71]
Citations
Cites
Intermolecular and Surface Forces
(2011) · Elsevier eBooks · doi:10.1016/b978-0-12-391927-4.10024-6 · Cited by 17,242
Intermolecular and Surface Forces
(2011) · Elsevier eBooks · doi:10.1016/c2011-0-05119-0 · Cited by 9,159
Crystal Structure of a Mammalian Voltage-Dependent Shaker Family K + Channel
Long, S. B., Campbell, E. B., & MacKinnon, R. (2005) · Science · doi:10.1126/science.1116269 · Cited by 2,159
Self-citationX-ray structure of a voltage-dependent K+ channel
Jiang, Y., Lee, A., Chen, J., Ruta, V., Cadène, M., Chait, B. T., & MacKinnon, R. (2003) · Nature · doi:10.1038/nature01580 · Cited by 1,798
Self-citationCrystal structure and mechanism of a calcium-gated potassium channel
Jiang, Y., Lee, A., Chen, J., Cadène, M., Chait, B. T., & MacKinnon, R. (2002) · Nature · doi:10.1038/417515a · Cited by 1,332
Self-citationVoltage Sensor of Kv1.2: Structural Basis of Electromechanical Coupling
Long, S. B., Campbell, E. B., & MacKinnon, R. (2005) · Science · doi:10.1126/science.1116270 · Cited by 982
Self-citationThe principle of gating charge movement in a voltage-dependent K+ channel
Jiang, Y., Ruta, V., Chen, J., Lee, A., & MacKinnon, R. (2003) · Nature · doi:10.1038/nature01581 · Cited by 781
Self-citationPhosphoinositide phosphatase activity coupled to an intrinsic voltage sensor
Murata, Y., Iwasaki, H., Sasaki, M., Inaba, K., & Okamura, Y. (2005) · Nature · doi:10.1038/nature03650 · Cited by 673
Miller, C. (1986) · Springer eBooks · doi:10.1007/978-1-4757-1361-9 · Cited by 605
Voltage gating of ion channels
Sigworth, F. J. (1994) · Quarterly Reviews of Biophysics · doi:10.1017/s0033583500002894 · Cited by 413
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Transport phenomena in nanofluidics
Schoch, R. B., Han, J., & Renaud, P. (2008) · Reviews of Modern Physics · doi:10.1103/revmodphys.80.839 · Cited by 1,973
Atomic structure of a voltage-dependent K+ channel in a lipid membrane-like environment
Long, S. B., Tao, X., Campbell, E. B., & MacKinnon, R. (2007) · Nature · doi:10.1038/nature06265 · Cited by 1,423
Self-citationMechanism of Voltage Gating in Potassium Channels
Jensen, M. Ø., Jogini, V., Borhani, D. W., Leffler, A. E., Dror, R. O., & Shaw, D. E. (2012) · Science · doi:10.1126/science.1216533 · Cited by 606
Ion Channel Voltage Sensors: Structure, Function, and Pathophysiology
Catterall, W. A. (2010) · Neuron · doi:10.1016/j.neuron.2010.08.021 · Cited by 570
Wang, G. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m805533200 · Cited by 483
Metadata
- Authors
- Schmidt, D., Jiang, Q.-X., & MacKinnon, R.
- Affiliations
- Howard Hughes Medical Institute (US)
- Corresponding author
- MacKinnon, Roderick
- Venue
- Nature
- Published
- 2006-11-29
- Volume
- 444
- Issue
- 7120
- Pages
- 775-779
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- 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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