ArticleProceedings of the National Academy of Sciences of the United States of America2008
Fluorescence detection of the movement of single KcsA subunits reveals cooperativity.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed.
- A Historical Outline of Fluorescence Spectroscopy in Ion Channel Research.Advances in experimental medicine and biology · 2026Review
- Studying KcsA Channel Clustering Using Single Channel Voltage-Clamp Fluorescence Imaging.Frontiers in physiology · 2022Article
- Queueing arrival and release mechanism for KThe journal of physiological sciences : JPS · 2019Article
- Site-Directed Fluorescence Approaches for Dynamic Structural Biology of Membrane Peptides and Proteins.Frontiers in molecular biosciences · 2019Review
- Rapid constriction of the selectivity filter underlies C-type inactivation in the KcsA potassium channel.The Journal of general physiology · 2018Article
- Article
- Conformational heterogeneity in closed and open states of the KcsA potassium channel in lipid bicelles.The Journal of general physiology · 2016Article
- Stepwise growth of surface-grafted DNA nanotubes visualized at the single-molecule level.Nature chemistry · 2015Article
- Integration and oligomerization of Bax protein in lipid bilayers characterized by single molecule fluorescence study.The Journal of biological chemistry · 2014Article
- Application of fluorescence resonance energy transfer in protein studies.Journal of molecular structure · 2014Article
- Quantifying the diffusion of membrane proteins and peptides in black lipid membranes with 2-focus fluorescence correlation spectroscopy.Biophysical journal · 2013Article
- Single-channel basis for the slow activation of the repolarizing cardiac potassium current, I(Ks).Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Modeling a ryanodine receptor N-terminal domain connecting the central vestibule and the corner clamp region.The Journal of biological chemistry · 2013Article
- Amphipathic antenna of an inward rectifier K+ channel responds to changes in the inner membrane leaflet.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Probing the energy landscape of activation gating of the bacterial potassium channel KcsA.PLoS computational biology · 2013Article
- A limited 4 Å radial displacement of the S4-S5 linker is sufficient for internal gate closing in Kv channels.The Journal of biological chemistry · 2012Article
- Single molecule fluorescence detection and tracking in mammalian cells: the state-of-the-art and future perspectives.International journal of molecular sciences · 2012Review
- Automating single subunit counting of membrane proteins in mammalian cells.The Journal of biological chemistry · 2012Article
- Mapping membrane protein structure with fluorescence.Current opinion in structural biology · 2012Review
- Single molecule fluorescence study of the Bacillus thuringiensis toxin Cry1Aa reveals tetramerization.The Journal of biological chemistry · 2011Article
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Authors and funding
4 authors.
Funding
Abstract
The prokaryotic KcsA channel is gated at the helical bundle crossing by intracellular protons and inactivates at the extracellular selectivity filter. The C-terminal transmembrane helix has to undergo a conformational change for potassium ions to access the central cavity. Whereas a partial opening of the tetrameric channel is suggested to be responsible for subconductance levels of ion channels, including KcsA, a cooperative opening of the 4 subunits is postulated as the final opening step. In this study, we used single-channel fluorescence spectroscopy of KcsA to directly observe the movement of each subunit and the temporal correlation between subunits. Purified KcsA channels labeled at the C terminus near the bundle crossing have been inserted into supported lipid bilayer, and the fluorescence traces analyzed by means of a cooperative or independent Markov model. The analysis revealed that the 4 subunits do not move fully independently but instead showed a certain degree of cooperativity. However, the 4 subunits do not simply open in 1 concerted step.
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