ArticleProceedings of the National Academy of Sciences of the United States of America2013
Amphipathic antenna of an inward rectifier K+ channel responds to changes in the inner membrane leaflet.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
43 citing papers in PubMed, 77 citations in OpenAlex.
- Leaflet-specific effects of charged lipids on a voltage-gated potassium channel.Journal of lipid research · 2025Article
- A short intrinsically disordered region at KtrB's N-terminus facilitates allosteric regulation of KNature communications · 2025Article
- Programmable Lipid Bilayer Tension-Control Apparatus for Quantitative Mechanobiology.ACS nano · 2024Article
- Asymmetric Lipid Bilayers and Potassium Channels Embedded Therein in the Contact Bubble Bilayer.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Cardiolipin binding enhances KcsA channel gating via both its specific and dianion-monoanion interchangeable sites.iScience · 2023Article
- Article
- "Force-From-Lipids" Dependence of the MscCG Mechanosensitive Channel Gating on Anionic Membranes.Microorganisms · 2023Article
- High-Resolution Magic Angle Spinning NMR of KcsA in Liposomes: The Highly Mobile C-Terminus.Biomolecules · 2022Article
- Studying KcsA Channel Clustering Using Single Channel Voltage-Clamp Fluorescence Imaging.Frontiers in physiology · 2022Article
- Probing the Structural Dynamics of the Activation Gate of KcsA Using Homo-FRET Measurements.International journal of molecular sciences · 2021Article
- Development of an automated system to measure ion channel currents using a surface-modified gold probe.Scientific reports · 2021Article
- Hysteresis of a Tension-Sensitive KJACS Au · 2021Article
- Conductance selectivity of NaProceedings of the National Academy of Sciences of the United States of America · 2021Article
- NMR studies of lipid regulation of the KBiochimica et biophysica acta. Biomembranes · 2021Article
- Distinct lipid bilayer compositions have general and protein-specific effects on K+ channel function.The Journal of general physiology · 2021Article
- Parallel Recordings of Transmembrane hERG Channel Currents Based on Solvent-Free Lipid Bilayer Microarray.Micromachines · 2021Article
- Druggable Lipid Binding Sites in Pentameric Ligand-Gated Ion Channels and Transient Receptor Potential Channels.Frontiers in physiology · 2021Review
- Physical and Chemical Interplay Between the Membrane and a Prototypical Potassium Channel Reconstituted on a Lipid Bilayer Platform.Frontiers in molecular neuroscience · 2021Review
- A Lipid Bilayer Formed on a Hydrogel Bead for Single Ion Channel Recordings.Micromachines · 2020Article
- Conformational equilibrium shift underlies altered KNature communications · 2020Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Membrane lipids modulate the function of membrane proteins. In the case of ion channels, they bias the gating equilibrium, although the underlying mechanism has remained elusive. Here we demonstrate that the N-terminal segment (M0) of the KcsA potassium channel mediates the effect of changes in the lipid milieu on channel gating. The M0 segment is a membrane-anchored amphipathic helix, bearing positively charged residues. In asymmetric membranes, the M0 helix senses the presence of negatively charged phospholipids on the inner leaflet. Upon gating, the M0 helix revolves around the axis of the helix on the membrane surface, inducing the positively charged residues to interact with the negative head groups of the lipids so as to stabilize the open conformation (i.e., the "roll-and-stabilize model"). The M0 helix is thus a charge-sensitive "antenna," capturing temporary changes in lipid composition in the fluidic membrane. This unique type of sensory device may be shared by various types of membrane proteins.
Indexed as
Identifiers
What OpenQuestion holds
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.