ArticleBiophysical journal2013
S3-S4 linker length modulates the relaxed state of a voltage-gated potassium channel.
Article in Biophysical journal, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 33 citations in OpenAlex.
- Molecular Determinants of Voltage-Dependent Gating in Kv11.1 Channels.Advances in experimental medicine and biology · 2026Review
- Structural basis for inhibition of the lysosomal two-pore channel TPC2 by a small molecule antagonist.Structure (London, England : 1993) · 2024Article
- Article
- The binding and mechanism of a positive allosteric modulator of Kv3 channels.Nature communications · 2024Article
- Cryo-EM structure of the human Kv3.1 channel reveals gating control by the cytoplasmic T1 domain.Nature communications · 2022Article
- The distinct role of the four voltage sensors of the skeletal CaV1.1 channel in voltage-dependent activation.The Journal of general physiology · 2021Article
- Molecular Insights Into the Gating Kinetics of the Cardiac hERG Channel, Illuminated by Structure and Molecular Dynamics.Frontiers in pharmacology · 2021Review
- Structural Dynamics of the Paddle Motif Loop in the Activated Conformation of KvAP Voltage Sensor.Biophysical journal · 2020Article
- Hysteretic Behavior in Voltage-Gated Channels.Frontiers in pharmacology · 2020Review
- Modulation of KFrontiers in pharmacology · 2020Article
- Modulation of hERG KFrontiers in pharmacology · 2020Review
- NMR Structural Analysis of Isolated Shaker Voltage-Sensing Domain in LPPG Micelles.Biophysical journal · 2019Article
- Extracellular protons accelerate hERG channel deactivation by destabilizing voltage sensor relaxation.The Journal of general physiology · 2019Article
- Electrostatic Tuning of a Potassium Channel in Electric Fish.Current biology : CB · 2018Article
- Functional characterization of Kv11.1 (hERG) potassium channels split in the voltage-sensing domain.Pflugers Archiv : European journal of physiology · 2018Article
- Nonsensing residues in S3-S4 linker's C terminus affect the voltage sensor set point in KThe Journal of general physiology · 2018Article
- Hysteresis in voltage-gated channels.Channels (Austin, Tex.) · 2017Review
- Stabilization of the Activated hERG Channel Voltage Sensor by Depolarization Involves the S4-S5 Linker.Biophysical journal · 2017Article
- Extracellular Linkers Completely Transplant the Voltage Dependence from Kv1.2 Ion Channels to Kv2.1.Biophysical journal · 2016Article
- The isolated voltage sensing domain of the Shaker potassium channel forms a voltage-gated cation channel.eLife · 2016Article
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
Voltage-sensing domains (VSDs) are membrane protein modules found in ion channels and enzymes that are responsible for a large number of fundamental biological tasks, such as neuronal electrical activity. The VSDs switch from a resting to an active conformation upon membrane depolarization, altering the activity of the protein in response to voltage changes. Interestingly, numerous studies describe the existence of a third distinct state, called the relaxed state, also populated at positive potentials. Although some physiological roles for the relaxed state have been suggested, little is known about the molecular determinants responsible for the development and modulation of VSD relaxation. Several lines of evidence have suggested that the linker (S3-S4 linker) between the third (S3) and fourth (S4) transmembrane segments of the VSD alters the equilibrium between resting and active conformations. By measuring gating currents from the Shaker potassium channel, we demonstrate here that shortening the S3-S4 linker stabilizes the relaxed state, whereas lengthening the linker or splitting it and coinjecting two fragments of the channel have little effect. We propose that natural variations of the length of the S3-S4 linker in various VSD-containing proteins may produce differential VSD relaxation in vivo.
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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.