ArticleThe Journal of biological chemistry2014
Do lipids show state-dependent affinity to the voltage-gated potassium channel KvAP?
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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Who cites it
8 citing papers in PubMed, 16 citations in OpenAlex.
- From Atoms to Neuronal Spikes: A Multiscale Simulation Framework.Journal of chemical theory and computation · 2026Review
- Leaflet-specific effects of charged lipids on a voltage-gated potassium channel.Journal of lipid research · 2025Article
- From Atoms to Neuronal Spikes: A Multi-Scale Simulation Framework.bioRxiv : the preprint server for biology · 2025Article
- Markov models and long-term memory in ion channels: A contradiction in terms?Biophysical journal · 2025Article
- A mutation in the S6 segment of the KvAP channel changes the secondary structure and alters ion channel activity in a lipid bilayer membrane.Amino acids · 2022Article
- Studying KcsA Channel Clustering Using Single Channel Voltage-Clamp Fluorescence Imaging.Frontiers in physiology · 2022Article
- Musculoskeletal Features without Ataxia Associated with a Novel de novo Mutation inBiomedicines · 2021Article
- Mechanosensitive gating of Kv channels.PloS one · 2015Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
As all integral membrane proteins, voltage-gated ion channels are embedded in a lipid matrix that regulates their channel behavior either by physicochemical properties or by direct binding. Because manipulation of the lipid composition in cells is difficult, we investigated the influence of different lipids on purified KvAP channels reconstituted in planar lipid bilayers of known composition. Lipids developed two distinct and independent effects on the KvAP channels; lipids interacting with the pore lowered the energy barriers for the final transitions, whereas voltage sensor-bound lipids shifted the midpoint of activation dependent on their electrostatic charge. Above all, the midpoint of activation was determined only by those lipids the channels came in contact with first after purification and can seemingly only be exchanged if the channel resides in the open state. The high affinity of the bound lipids to the binding site has implications not only on our understanding of the gating mechanism but also on the general experimental design of any lipid dependence study.
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Registered trials
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