ArticleThe journal of physical chemistry. B2011
Structural dynamics of the S4 voltage-sensor helix in lipid bilayers lacking phosphate groups.
Article in The journal of physical chemistry. B, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
9 citing papers in PubMed.
- DOTAP: Structure, hydration, and the counterion effect.Biophysical journal · 2023Article
- Tracking Membrane Protein Dynamics in Real Time.The Journal of membrane biology · 2021Review
- Musculoskeletal Features without Ataxia Associated with a Novel de novo Mutation inBiomedicines · 2021Article
- TRP Channels, Conformational Flexibility, and the Lipid Membrane.The Journal of membrane biology · 2020Review
- Uptake dynamics in the Lactose permease (LacY) membrane protein transporter.Scientific reports · 2018Article
- Membrane Anchoring and Ion-Entry Dynamics in P-type ATPase Copper Transport.Biophysical journal · 2016Article
- The Molecular Basis of Polyunsaturated Fatty Acid Interactions with the Shaker Voltage-Gated Potassium Channel.PLoS computational biology · 2016Article
- Interactions between ether phospholipids and cholesterol as determined by scattering and molecular dynamics simulations.The journal of physical chemistry. B · 2012Article
- Cholesterol-Dependent Gating Effects on Ion Channels.Advances in experimental medicine and biologyReview
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors.
Funding
Abstract
Voltage-dependent K(+) (Kv) channels require lipid phosphates for functioning. The S4 helix, which carries the gating charges in the voltage-sensing domain (VSD), inserts into membranes while being stabilized by a protein-lipid interface in which lipid phosphates play an essential role. To examine the physical basis of the protein-lipid interface in the absence of lipid phosphates, we performed molecular dynamics (MD) simulations of a KvAP S4 variant (S4mut) in bilayers with and without lipid phosphates. We find that, in dioleoyltrimethylammoniumpropane (DOTAP) bilayers lacking lipid phosphates, the gating charges are solvated by anionic counterions and, hence, lack the bilayer support provided by phosphate-containing palmitoyloleoylglycerophosphocholine (POPC) bilayers. The result is a water-permeable bilayer with significantly smaller deformations around the peptide. Together, these results provide an explanation for the nonfunctionality of VSDs in terms of a destabilizing protein-lipid interface.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.