ArticleJournal of molecular biology2012
Structural interactions between lipids, water and S1-S4 voltage-sensing domains.
Article in Journal of molecular biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
- AI-Resolved Protein Energy Landscapes, Electrodynamics, and Fluidic Microcircuits as a Unified Framework for Predicting Neurodegeneration.International journal of molecular sciences · 2026Review
- Solid-state NMR of membrane peptides and proteins in the lipid cubic phase.Biophysical journal · 2025Article
- Special issue for Klaus Gawrisch.Biophysical journal · 2023Article
- Beyond Structural Biology to Functional Biology: Solid-State NMR Experiments and Strategies for Understanding the M2 Proton Channel Conductance.The journal of physical chemistry. B · 2017Article
- Probing Hydronium Ion Histidine NH Exchange Rate Constants in the M2 Channel via Indirect Observation of Dipolar-DephasedJournal of the American Chemical Society · 2016Article
- Article
- Voltage Sensing in Membranes: From Macroscopic Currents to Molecular Motions.The Journal of membrane biology · 2015Review
- Mechanosensitive gating of Kv channels.PloS one · 2015Review
- Cardiolipin interaction with subunit c of ATP synthase: solid-state NMR characterization.Biochimica et biophysica acta · 2015Article
- Structural interactions of a voltage sensor toxin with lipid membranes.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Do lipids show state-dependent affinity to the voltage-gated potassium channel KvAP?The Journal of biological chemistry · 2014Article
- Structural basis of lipid-driven conformational transitions in the KvAP voltage-sensing domain.Nature structural & molecular biology · 2014Article
- Conformational transition of membrane-associated terminally acylated HIV-1 Nef.Structure (London, England : 1993) · 2013Article
- Tuning voltage-gated channel activity and cellular excitability with a sphingomyelinase.The Journal of general physiology · 2013Article
- The design principle of paddle motifs in voltage sensors.Nature structural & molecular biology · 2013Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
Membrane proteins serve crucial signaling and transport functions, yet relatively little is known about their structures in membrane environments or how lipids interact with these proteins. For voltage-activated ion channels, X-ray structures suggest that the mobile voltage-sensing S4 helix would be exposed to the membrane, and functional studies reveal that lipid modification can profoundly alter channel activity. Here, we use solid-state NMR to investigate structural interactions of lipids and water with S1-S4 voltage-sensing domains and to explore whether lipids influence the structure of the protein. Our results demonstrate that S1-S4 domains exhibit extensive interactions with lipids and that these domains are heavily hydrated when embedded in a membrane. We also find evidence for preferential interactions of anionic lipids with S1-S4 domains and that these interactions have lifetimes on the timescale of ≤ 10(-3)s. Arg residues within S1-S4 domains are well hydrated and are positioned in close proximity to lipids, exhibiting local interactions with both lipid headgroups and acyl chains. Comparative studies with a positively charged lipid lacking a phosphodiester group reveal that this lipid modification has only modest effects on the structure and hydration of S1-S4 domains. Taken together, our results demonstrate that Arg residues in S1-S4 voltage-sensing domains reside in close proximity to the hydrophobic interior of the membrane yet are well hydrated, a requirement for carrying charge and driving protein motions in response to changes in membrane voltage.
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Registered trials
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